ΠŸΠΎΠΌΠΎΡ‰ΡŒ Π² написании студСнчСских Ρ€Π°Π±ΠΎΡ‚
АнтистрСссовый сСрвис

Π˜Π·ΡƒΡ‡Π΅Π½ΠΈΠ΅ взаимодСйствия Ρ€50-ΠΌΠ°ΠΆΠΎΡ€Π½ΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ° мРНП β€” с РНК

Π”ΠΈΡΡΠ΅Ρ€Ρ‚Π°Ρ†ΠΈΡΠŸΠΎΠΌΠΎΡ‰ΡŒ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈΠ£Π·Π½Π°Ρ‚ΡŒ ΡΡ‚ΠΎΠΈΠΌΠΎΡΡ‚ΡŒΠΌΠΎΠ΅ΠΉ Ρ€Π°Π±ΠΎΡ‚Ρ‹

ΠŸΡ€Π΅ΠΆΠ΄Π΅ всСго, я Π³Π»ΡƒΠ±ΠΎΠΊΠΎ Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€Π΅Π½ ΠΌΠΎΠ΅ΠΌΡƒ Π½Π°ΡƒΡ‡Π½ΠΎΠΌΡƒ Ρ€ΡƒΠΊΠΎΠ²ΠΎΠ΄ΠΈΡ‚Π΅Π»ΡŽ Π›ΡŒΠ²Ρƒ ΠŸΠ°Π²Π»ΠΎΠ²ΠΈΡ‡Ρƒ ΠžΠ²Ρ‡ΠΈΠ½Π½ΠΈΠΊΠΎΠ²Ρƒ. Он Π²Π·ΡΠ» мСня Π² ΡΠ²ΠΎΡŽ Π»Π°Π±ΠΎΡ€Π°Ρ‚ΠΎΡ€ΠΈΡŽ Π΅Ρ‰Π΅ ΡΠΎΠ²Π΅Ρ€ΡˆΠ΅Π½Π½ΠΎ Π½Π΅ΠΎΠ±ΡƒΡ‡Π΅Π½Π½Ρ‹ΠΌ ΠΈ «Π·Π΅Π»Π΅Π½Ρ‹ΠΌ». Π’ Ρ‚ΠΎΠΌ, Ρ‡Ρ‚ΠΎ я ΡΠ΅Π³ΠΎΠ΄Π½Ρ собой ΠΏΡ€Π΅Π΄ΡΡ‚Π°Π²Π»ΡΡŽ, ΠΊΠ°ΠΊ Π½Π°ΡƒΡ‡Π½Ρ‹ΠΉ Ρ€Π°Π±ΠΎΡ‚Π½ΠΈΠΊ, огромная Π΅Π³ΠΎ заслуга. Он ΠΏΡ€ΠΈΡΡ‚Π°Π»ΡŒΠ½ΠΎ ΠΈ Π²Π½ΠΈΠΌΠ°Ρ‚Π΅Π»ΡŒΠ½ΠΎ Ρ€ΡƒΠΊΠΎΠ²ΠΎΠ΄ΠΈΠ» ΠΊΠ°ΠΆΠ΄Ρ‹ΠΌ этапом ΠΌΠΎΠ΅ΠΉ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Ρ‚Π΅Π»ΡŒΡΠΊΠΎΠΉ Ρ€Π°Π±ΠΎΡ‚Ρ‹. НСоцСним Π΅Π³ΠΎ Π²ΠΊΠ»Π°Π΄ ΠΈ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ тСкста диссСртации. ОсобСнно я Ρ…ΠΎΡ‡Ρƒ… Π§ΠΈΡ‚Π°Ρ‚ΡŒ Π΅Ρ‰Ρ‘ >

Π˜Π·ΡƒΡ‡Π΅Π½ΠΈΠ΅ взаимодСйствия Ρ€50-ΠΌΠ°ΠΆΠΎΡ€Π½ΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ° мРНП β€” с РНК (Ρ€Π΅Ρ„Π΅Ρ€Π°Ρ‚, курсовая, Π΄ΠΈΠΏΠ»ΠΎΠΌ, ΠΊΠΎΠ½Ρ‚Ρ€ΠΎΠ»ΡŒΠ½Π°Ρ)

Π‘ΠΎΠ΄Π΅Ρ€ΠΆΠ°Π½ΠΈΠ΅

  • ΠžΠ‘Π—ΠžΠ  Π›Π˜Π’Π•Π ΠΠ’Π£Π Π« ΠœΠΠ–ΠžΠ ΠΠ«Π• Π‘Π•Π›ΠšΠ˜ ЯДЕРНЫΠ₯ И Π¦Π˜Π’ΠžΠŸΠ›ΠΠ—ΠœΠΠ’Π˜Π§Π•Π‘ΠšΠ˜Π₯ мРНП
  • Π‘Π’Π ΠžΠ•ΠΠ˜Π• И Π€Π£ΠΠšΠ¦Π˜ΠžΠΠ˜Π ΠžΠ’ΠΠΠ˜Π•
  • I. Π“Π΅Ρ‚Π΅Ρ€ΠΎΠ³Π΅Π½Π½Ρ‹Π΅ ядСрныС Ρ€ΠΈΠ±ΠΎΠ½ΡƒΠΊΠ»Π΅ΠΎΠΏΡ€ΠΎΡ‚Π΅ΠΈΠ΄Π½Ρ‹Π΅ частицы (гяРНП)
  • 1. Π˜ΡΡ‚ΠΎΡ€ΠΈΡ открытия гяРНП
  • 2. Π‘Π΅Π»ΠΊΠΈ гяРНП
    • 2. 1. ΠžΠ±Ρ‰ΠΈΠ΅ характСристики Π±Π΅Π»ΠΊΠΎΠ² гяРНП
    • 2. 2. Π”ΠΎΠΌΠ΅Π½Ρ‹ Π±Π΅Π»ΠΊΠΎΠ² гяРНП
      • 2. 2. 1. РНК-ΡΠ²ΡΠ·Ρ‹Π²Π°ΡŽΡ‰ΠΈΠΉ Π΄ΠΎΠΌΠ΅Π½ (RBD)
      • 2. 2. 2. КН-Π΄ΠΎΠΌΠ΅Π½
      • 2. 2. 3. Π’ΡΠΏΠΎΠΌΠΎΠ³Π°Ρ‚Π΅Π»ΡŒΠ½Ρ‹Π΅ Π΄ΠΎΠΌΠ΅Π½Ρ‹ (auxiliary domains)
    • 2. 3. ΠšΠΎΡ€ΠΎΠ²Ρ‹Π΅ Π±Π΅Π»ΠΊΠΈ гяРНП
      • 2. 3. 1. А/Π’ Π³Ρ€ΡƒΠΏΠΏΠ° Π±Π΅Π»ΠΊΠΎΠ² гяРНП
      • 2. 3. 2. Π“Ρ€ΡƒΠΏΠΏΠ° Π‘ Π±Π΅Π»ΠΊΠΎΠ² гяРНП
    • 2. 4. ΠŸΡ€ΠΎΡ‡ΠΈΠ΅ «Π½Π΅ ΠΊΠΎΡ€ΠΎΠ²Ρ‹Π΅» Π±Π΅Π»ΠΊΠΈ гяРНП
  • 3. Π£ΠΏΠ°ΠΊΠΎΠ²ΠΊΠ° гяРНК ΠΈ ΡΡ‚Ρ€ΡƒΠΊΡ‚ΡƒΡ€Π° гяРНП
  • 4. Вранспорт мРНК ΠΈΠ· ΡΠ΄Ρ€Π° Π² Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡƒ
  • II. ЦитоплазматичСскиС ΠΌΠ°Ρ‚Ρ€ΠΈΡ‡Π½Ρ‹Π΅ Ρ€ΠΈΠ±ΠΎΠ½ΡƒΠΊΠ»Π΅ΠΎΠΏΡ€ΠΎΡ‚Π΅ΠΈΠ΄Π½Ρ‹Π΅ частицы (мРНП)
  • 1. Π˜ΡΡ‚ΠΎΡ€ΠΈΡ открытия цитоплазматичСских мРНП
  • 2. ΠžΡΠ½ΠΎΠ²Π½Ρ‹Π΅ характСристики мРНП
  • 3. ΠœΠ°ΠΆΠΎΡ€Π½Ρ‹Π΅ Π±Π΅Π»ΠΊΠΈ цитоплазматичСских мРНП
    • 3. 1. Поли (А)-ΡΠ²ΡΠ·Ρ‹Π²Π°ΡŽΡ‰ΠΈΠΉ Π±Π΅Π»ΠΎΠΊ РАВР
      • 3. 1. 1. Π‘Ρ‚Ρ€ΡƒΠΊΡ‚ΡƒΡ€Π° РАВР ΠΈ Π΅Π³ΠΎ связываниС с ΠΌΠ ΠΠš
      • 3. 1. 2. Π€ΡƒΠ½ΠΊΡ†ΠΈΠΈ РАВР
    • 3. 2. ΠœΠ°ΠΆΠΎΡ€Π½Ρ‹ΠΉ Π±Π΅Π»ΠΎΠΊ цитоплазматичСских мРНП Ρ€ ΠΈ Π΅Π³ΠΎ Π³ΠΎΠΌΠΎΠ»ΠΎΠ³ΠΈ с Π΄ΠΎΠΌΠ΅Π½Π°ΠΌΠΈ Ρ…ΠΎΠ»ΠΎΠ΄ΠΎΠ²ΠΎΠ³ΠΎ шока (CSD-Π±Π΅Π»ΠΊΠΈ)
      • 3. 2. 1. ΠžΠ±Π½Π°Ρ€ΡƒΠΆΠ΅Π½ΠΈΠ΅ Ρ€50 ΠΈ Π΄Ρ€ΡƒΠ³ΠΈΡ… Ρ‡Π»Π΅Π½ΠΎΠ² сСмСйства Π±Π΅Π»ΠΊΠΎΠ² с Π΄ΠΎΠΌΠ΅Π½Π°ΠΌΠΈ Ρ…ΠΎΠ»ΠΎΠ΄ΠΎΠ²ΠΎΠ³ΠΎ шока
      • 3. 2. 2. Π‘Ρ‚Ρ€ΠΎΠ΅Π½ΠΈΠ΅ Ρ€
      • 3. 2. 3. Π‘Ρ‚Ρ€ΡƒΠΊΡ‚ΡƒΡ€Π° Π³Π΅Π½ΠΎΠ² Ρ€50 ΠΈ Π΅Π³ΠΎ Π³ΠΎΠΌΠΎΠ»ΠΎΠ³ΠΎΠ² Ρƒ ΠΏΠΎΠ·Π²ΠΎΠ½ΠΎΡ‡Π½Ρ‹Ρ…
      • 3. 2. 4. ВзаимодСйствиС Ρ€50 с Π ΠΠš
      • 3. 2. 5. Ρ€50 Π² Π±ΠΈΠΎΠ³Π΅Π½Π΅Π·Π΅ ΠΈ Ρ„ΡƒΠ½ΠΊΡ†ΠΈΠΎΠ½ΠΈΡ€ΠΎΠ²Π°Π½ΠΈΠΈ мРНК
      • 3. 2. 6. ИзмСнСниС ΠΊΠΎΠ½Ρ†Π΅Π½Ρ‚Ρ€Π°Ρ†ΠΈΠΈ Ρ€50 Π² ΠΊΠ»Π΅Ρ‚ΠΊΠ΅ ΠΈ Π΅Π΅ ΠΊΠΎΠΌΠΏΠ°Ρ€Ρ‚ΠΌΠ΅Π½Ρ‚Π°Ρ…
  • 4. Бтруктурная организация цитоплазматичСских мРНП
  • Π­ΠšΠ‘ΠŸΠ•Π Π˜ΠœΠ•ΠΠ’ΠΠ›Π¬ΠΠΠ― ЧАБВЬ ΠœΠΠ’Π•Π Π˜ΠΠ›Π« И ΠœΠ•Π’ΠžΠ”Π«
  • 1. Π’Ρ‹Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Ρ€Π΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½Ρ‚Π½ΠΎΠ³ΠΎ Ρ€50 ΠΈΠ· Escherichia col
  • 2. ΠŸΠΎΠ»ΡƒΡ‡Π΅Π½ΠΈΠ΅ Ρ„Ρ€Π°Π³ΠΌΠ΅Π½Ρ‚ΠΎΠ² Ρ€
  • 3. Π’Ρ‹Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΏΠ»Π°Π·ΠΌΠΈΠ΄Π½ΠΎΠΉ Π”ΠΠš ΠΈΠ· Escherichia col
  • 4. РСстрикция ΠΏΠ»Π°Π·ΠΌΠΈΠ΄Ρ‹
  • 5. АналитичСский элСктрофорСз Π½ΡƒΠΊΠ»Π΅ΠΈΠ½ΠΎΠ²Ρ‹Ρ… кислот Π² Π³Π΅Π»Π΅ Π°Π³Π°Ρ€ΠΎΠ·Ρ‹
  • 6. ΠŸΠΎΠ»ΡƒΡ‡Π΅Π½ΠΈΠ΅ транскриптов РНК in vitro
  • 7. Π­Π»Π΅ΠΊΡ‚Ρ€ΠΎΡ„ΠΎΡ€Π΅Π· РНК Π² ΠΏΠΎΠ»ΠΈΠ°ΠΊΡ€ΠΈΠ»Π°ΠΌΠΈΠ΄Π½ΠΎΠΌ Π³Π΅Π»Π΅ Π² ΠΏΡ€ΠΈΡΡƒΡ‚ствии ΠΌΠΎΡ‡Π΅Π²ΠΈΠ½Ρ‹
  • 8. ΠŸΡ€Π΅ΠΏΠ°Ρ€Π°Ρ‚ΠΈΠ²Π½ΠΎΠ΅ Π²Ρ‹Π΄Π΅Π»Π΅Π½ΠΈΠ΅ РНК ΠΈΠ· ΠΏΠΎΠ»ΠΈΠ°ΠΊΡ€ΠΈΠ»Π°ΠΌΠΈΠ΄Π½ΠΎΠ³ΠΎ гСля
  • 9. ΠŸΡ€ΠΎΠ²Π΅Π΄Π΅Π½ΠΈΠ΅ ΠΏΠΎΠ»ΠΈΠΌΠ΅Ρ€Π°Π·Π½ΠΎΠΉ Ρ†Π΅ΠΏΠ½ΠΎΠΉ Ρ€Π΅Π°ΠΊΡ†ΠΈΠΈ (ПЦР)
  • 10. ΠœΠ΅Ρ‡Π΅Π½ΠΈΠ΅ Π”ΠΠš 32Π  ΠΏΠΎ 5' ΠΊΠΎΠ½Ρ†Ρƒ
  • 11. Π­Π»Π΅ΠΊΡ‚Ρ€ΠΎΡ„ΠΎΡ€Π΅Π· Π±Π΅Π»ΠΊΠΎΠ² Π² ΠΏΠΎΠ»ΠΈΠ°ΠΊΡ€ΠΈΠ»Π°ΠΌΠΈΠ΄Π½ΠΎΠΌ Π³Π΅Π»Π΅ Π² ΠΏΡ€ΠΈΡΡƒΡ‚ствии SDS
  • 12. Π‘Π±ΠΎΡ€ΠΊΠ° комплСксов мРНК с Ρ€50 ΠΈ ΠΈΡ… Π°Π½Π°Π»ΠΈΠ· Ρ†Π΅Π½Ρ‚Ρ€ΠΈΡ„ΡƒΠ³ΠΈΡ€ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π² Π³Ρ€Π°Π΄ΠΈΠ΅Π½Ρ‚Π΅ ΠΊΠΎΠ½Ρ†Π΅Π½Ρ‚Ρ€Π°Ρ†ΠΈΠΈ сахарозы
  • 13. Π¦Π΅Π½Ρ‚Ρ€ΠΈΡ„ΡƒΠ³ΠΈΡ€ΠΎΠ²Π°Π½ΠΈΠ΅ комплСксов мРНК с Ρ€ Π² Π³Ρ€Π°Π΄ΠΈΠ΅Π½Ρ‚Π΅ плотности CsCl
  • 14. ΠžΠΏΡ€Π΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ Ρ‡Π΅Ρ‚Π²Π΅Ρ€Ρ‚ΠΈΡ‡Π½ΠΎΠΉ структуры Ρ€ Π² ΠΊΠΎΠΌΠΏΠ»Π΅ΠΊΡΠ΅ с ΠΌΠ ΠΠš ΠΌΠ΅Ρ‚ΠΎΠ΄ΠΎΠΌ сшивки Π³Π»ΡƒΡ‚Π°Ρ€ΠΎΠ²Ρ‹ΠΌ альдСгидом
  • 15. ИсслСдованиС взаимодСйствия Π±Π΅Π»ΠΊΠ° с Π ΠΠš ΠΌΠ΅Ρ‚ΠΎΠ΄ΠΎΠΌ замСдлСния подвиТности РНК Π² Π³Π΅Π»Π΅ (gel-shift assay)
  • 16. ΠžΠΏΡ€Π΅Π΄Π΅Π»Π΅Π½ΠΈΠ΅ ΠΎΡ‚Π½ΠΎΡΠΈΡ‚Π΅Π»ΡŒΠ½Ρ‹Ρ… ΠΊΠΎΠ½Ρ‚Π°ΠΊΡ‚ΠΎΠ² Π΄ΠΎΠΌΠ΅Π½ΠΎΠ² Ρ€50 с ΠΌΠ ΠΠš ΠΌΠ΅Ρ‚ΠΎΠ΄ΠΎΠΌ ΡƒΠ»ΡŒΡ‚Ρ€Π°Ρ„ΠΈΠΎΠ»Π΅Ρ‚ΠΎΠ²Ρ‹Ρ… сшивок Π±Π΅Π»ΠΊΠ° с Π -ΠΌΠ΅Ρ‡Π΅Π½Π½ΠΎΠΉ РНК
  • 17. ИсслСдованиС распрСдСлСния Π±Π΅Π»ΠΊΠ° Ρ€ Π²ΠΎ Ρ„ракциях Π³Ρ€Π°Π΄ΠΈΠ΅Π½Ρ‚Π° CsCl ΠΌΠ΅Ρ‚ΠΎΠ΄ΠΎΠΌ Western-dot
  • 18. ΠžΡ‚ΠΆΠΈΠ³ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ Π½ΡƒΠΊΠ»Π΅ΠΈΠ½ΠΎΠ²Ρ‹Ρ… кислот Π² ΠΏΡ€ΠΈΡΡƒΡ‚ствии Ρ€
  • 19. ИсслСдованиС ΠΎΠ±ΠΌΠ΅Π½Π° ΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ
  • РНК Π² ΠΏΡ€ΠΈΡΡƒΡ‚ствии Ρ€50 ΠΈ Π΅Π³ΠΎ Ρ„Ρ€Π°Π³ΠΌΠ΅Π½Ρ‚ΠΎΠ²
  • РЕЗУЛЬВАВЫ
  • 1. ИсслСдованиС комплСксов Ρ€50 с ΠΌΠ ΠΠš
    • 1. 1. БСдимСнтационная характСристика комплСксов Ρ€50 с ΠΌΠ ΠΠš
    • 1. 2. ΠŸΠ»ΠΎΡ‚Π½ΠΎΡΡ‚Π½ΠΎΠ΅ распрСдСлСниС комплСксов Ρ€50 с ΠΌΠ ΠΠš Π² Π³Ρ€Π°Π΄ΠΈΠ΅Π½Ρ‚Π΅ CsCl
    • 1. 3. ΠšΠΎΠΌΠΏΠ»Π΅ΠΊΡΡ‹ Ρ€50 с ΠΌΠ ΠΠš Π½Π΅ΡΡ‚Π°Π±ΠΈΠ»ΡŒΠ½Ρ‹, ΠΈ Π±Π΅Π»ΠΎΠΊ Π»Π΅Π³ΠΊΠΎ ΠΏΠ΅Ρ€Π΅Ρ…ΠΎΠ΄ΠΈΡ‚ с ΠΎΠ΄Π½ΠΎΠΉ ΠΌΠΎΠ»Π΅ΠΊΡƒΠ»Ρ‹ мРНК Π½Π° Π΄Ρ€ΡƒΠ³ΡƒΡŽ
    • 1. 4. ΠŸΡ€ΠΈ Π½ΠΈΠ·ΠΊΠΈΡ… ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡΡ… Ρ€50/мРНК Π±Π΅Π»ΠΎΠΊ связываСтся с ΠΌΠ ΠΠš ΠΊΠ°ΠΊ ΠΌΠΎΠ½ΠΎΠΌΠ΅Ρ€, Π² Ρ‚ΠΎ Π²Ρ€Π΅ΠΌΡ ΠΊΠ°ΠΊ ΠΏΡ€ΠΈ высоких ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡΡ… Ρ€50 ΠΎΠ±Ρ€Π°Π·ΡƒΠ΅Ρ‚ Π½Π° ΠΌΠ ΠΠš ΠΌΡƒΠ»ΡŒΡ‚ΠΈΠΌΠ΅Ρ€Ρ‹

    1.5. ΠŸΡ€ΠΈ Π½ΠΈΠ·ΠΊΠΈΡ… ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡΡ… Ρ€50/мРНК Π±Π΅Π»ΠΎΠΊ связываСтся с ΠΌΠ ΠΠš двумя РНК-ΡΠ²ΡΠ·Ρ‹Π²Π°ΡŽΡ‰ΠΈΠΌΠΈ Π΄ΠΎΠΌΠ΅Π½Π°ΠΌΠΈ, Π² Ρ‚ΠΎ Π²Ρ€Π΅ΠΌΡ ΠΊΠ°ΠΊ ΠΏΡ€ΠΈ высоких значСниях этого ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡ Π±Π΅Π»ΠΎΠΊ взаимодСйствуСт с ΠΌΠ ΠΠš прСимущСствСнно N-ΠΊΠΎΠ½Ρ†Π΅Π²ΠΎΠΉ Ρ‡Π°ΡΡ‚ΡŒΡŽ ΠΌΠΎΠ»Π΅ΠΊΡƒΠ»Ρ‹ с Π΄ΠΎΠΌΠ΅Π½ΠΎΠΌ Ρ…ΠΎΠ»ΠΎΠ΄ΠΎΠ²ΠΎΠ³ΠΎ шока.

    2. ВлияниС Ρ€50 Π½Π° Π²Ρ‚ΠΎΡ€ΠΈΡ‡Π½ΡƒΡŽ структуру РНК.

    2.1. Ρ€50 ускоряСт ΠΎΡ‚ΠΆΠΈΠ³ Π²Π·Π°ΠΈΠΌΠΎΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ РНК.

    2.2. Ρ€50 ускоряСт ΠΎΠ±ΠΌΠ΅Π½ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ Π² ΠΌΠΎΠ»Π΅ΠΊΡƒΠ»Π°Ρ…

    РНК ΠΈ ΠΏΡ€ΠΈΠ²ΠΎΠ΄ΠΈΡ‚ ΠΊ ΠΎΠ±Ρ€Π°Π·ΠΎΠ²Π°Π½ΠΈΡŽ Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ протяТСнных дуплСксов.

    2.3. Ρ€50 Π²Ρ‹Π·Ρ‹Π²Π°Π΅Ρ‚ ΠΏΠ»Π°Π²Π»Π΅Π½ΠΈΠ΅ ΠΈΠ»ΠΈ, Π½Π°ΠΎΠ±ΠΎΡ€ΠΎΡ‚, ΠΎΡ‚ΠΆΠΈΠ³

    РНК Π² Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡ‚ΠΈ ΠΎΡ‚ ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡ Ρ€50/РНК.

    2.4. Ρ€50 ускоряСт ΠΎΡ‚ΠΆΠΈΠ³ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ Π”ΠΠš.

    2.5. ЀосфорилированиС in vitro Π±Π΅Π»ΠΊΠ° Ρ€50 ΠΊΠ°Π·Π΅ΠΈΠ½ΠΊΠΈΠ½Π°Π·ΠΎΠΉ II сниТаСт Π΅Π³ΠΎ Π”ΠΠš-ΠΎΡ‚ΠΆΠΈΠ³Π°ΡŽΡ‰ΡƒΡŽ Π°ΠΊΡ‚ΠΈΠ²Π½ΠΎΡΡ‚ΡŒ, Π½ΠΎ Π½Π΅ Π²Π»ΠΈΡΠ΅Ρ‚ Π½Π° ΠΎΡ‚ΠΆΠΈΠ³ РНК.

    ΠžΠ‘Π‘Π£Π–Π”Π•ΠΠ˜Π• Π Π•Π—Π£Π›Π¬Π’ΠΠ’ΠžΠ’.

    1. Ρ€50 — основной ΡΡ‚Ρ€ΡƒΠΊΡ‚ΡƒΡ€ΠΎΠΎΠ±Ρ€Π°Π·ΡƒΡŽΡ‰ΠΈΠΉ Π±Π΅Π»ΠΎΠΊ цитоплазматичСских мРНП эукариотичСских ΠΊΠ»Π΅Ρ‚ΠΎΠΊ.

    2. Ρ€50 — ΡˆΠ°ΠΏΠ΅Ρ€ΠΎΠ½ Π½ΡƒΠΊΠ»Π΅ΠΈΠ½ΠΎΠ²Ρ‹Ρ… кислот.

    Π’Π«Π’ΠžΠ”Π«.

    Π‘Π›ΠΠ“ΠžΠ”ΠΠ ΠΠžΠ‘Π’Π˜.

ΠœΠΎΠ»Π΅ΠΊΡƒΠ»Ρ‹ мРНК эукариотичСской ΠΊΠ»Π΅Ρ‚ΠΊΠΈ ΡΠΈΠ½Ρ‚Π΅Π·ΠΈΡ€ΡƒΡŽΡ‚ΡΡ Π² ΠΊΠ»Π΅Ρ‚ΠΎΡ‡Π½ΠΎΠΌ ядрС Π² Π²ΠΈΠ΄Π΅ ΠΏΡ€Π΅Π΄ΡˆΠ΅ΡΡ‚Π²Π΅Π½Π½ΠΈΠΊΠΎΠ², ΠΎΠ±Ρ€Π°Π·ΡƒΡŽΡ‰ΠΈΡ… Ρ„Ρ€Π°ΠΊΡ†ΠΈΡŽ Π³Π΅Ρ‚Π΅Ρ€ΠΎΠ³Π΅Π½Π½Ρ‹Ρ… ядСрных РНК (гяРНК). Π’Π°ΠΌ ΠΆΠ΅ Π² ΡΠ΄Ρ€Π΅ эти ΠΏΡ€Π΅Π΄ΡˆΠ΅ΡΡ‚Π²Π΅Π½Π½ΠΈΠΊΠΈ ΠΏΡ€ΠΎΡ†Π΅ΡΡΠΈΡ€ΡƒΡŽΡ‚ΡΡ Π΄ΠΎ Π·Ρ€Π΅Π»Ρ‹Ρ… мРНК, ΠΊΠΎΡ‚ΠΎΡ€Ρ‹Π΅ пСрСносятся Ρ‡Π΅Ρ€Π΅Π· ядСрныС ΠΏΠΎΡ€Ρ‹ Π² Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡƒ. Π’ Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΠ΅ мРНК ΠΌΠΎΠ³ΡƒΡ‚ ΠΏΡ€Π΅Π±Ρ‹Π²Π°Ρ‚ΡŒ Π½Π΅ΠΊΠΎΡ‚ΠΎΡ€ΠΎΠ΅ врСмя (ΠΈΠ½ΠΎΠ³Π΄Π° ΠΎΡ‡Π΅Π½ΡŒ Π΄Π»ΠΈΡ‚Π΅Π»ΡŒΠ½ΠΎΠ΅) Π² Π½Π΅Ρ‚ранслируСмом состоянии ΠΈΠ»ΠΈ Π°ΡΡΠΎΡ†ΠΈΠΈΡ€ΠΎΠ²Π°Ρ‚ΡŒ с Ρ€ΠΈΠ±ΠΎΡΠΎΠΌΠ°ΠΌΠΈ ΠΈ ΡΠ»ΡƒΠΆΠΈΡ‚ΡŒ ΠΌΠ°Ρ‚Ρ€ΠΈΡ†Π°ΠΌΠΈ для Π±Π΅Π»ΠΊΠΎΠ²ΠΎΠ³ΠΎ синтСза. Π’Π°ΠΊΠΈΠΌ ΠΎΠ±Ρ€Π°Π·ΠΎΠΌ, ΠΌΠΎΠ»Π΅ΠΊΡƒΠ»Ρ‹ мРНК ΠΈΠΌΠ΅ΡŽΡ‚ «ΡΠ΄Π΅Ρ€Π½Ρ‹ΠΉ» ΠΈ «Ρ†ΠΈΡ‚оплазматичСский» ΠΏΠ΅Ρ€ΠΈΠΎΠ΄Ρ‹ своСй истории.

Π―Π΄Π΅Ρ€Π½Ρ‹Π΅ ΠΏΡ€Π΅Π΄ΡˆΠ΅ΡΡ‚Π²Π΅Π½Π½ΠΈΠΊΠΈ ΠΈ Π·Ρ€Π΅Π»Ρ‹Π΅ мРНК ассоциированы с Π±Π΅Π»ΠΊΠ°ΠΌΠΈ ΠΈ ΠΎΠ±Ρ€Π°Π·ΡƒΡŽΡ‚ с Π½ΠΈΠΌΠΈ Ρ€ΠΈΠ±ΠΎΠ½ΡƒΠΊΠ»Π΅ΠΎΠΏΡ€ΠΎΡ‚Π΅ΠΈΠ΄Π½Ρ‹Π΅ частицы с ΡƒΠ½ΠΈΠΊΠ°Π»ΡŒΠ½Ρ‹ΠΌΠΈ свойствами. Π˜ΡΡ‚ΠΎΡ€ΠΈΡ‡Π΅ΡΠΊΠΈ ΠΏΠ΅Ρ€Π²Ρ‹ΠΌΠΈ Π² 1964 Π³ Π±Ρ‹Π»ΠΈ ΠΎΠ±Π½Π°Ρ€ΡƒΠΆΠ΅Π½Ρ‹ ΠΈ ΠΎΡ…Π°Ρ€Π°ΠΊΡ‚Π΅Ρ€ΠΈΠ·ΠΎΠ²Π°Π½Ρ‹ частицы, содСрТащиС цитоплазматичСскиС нСтранслируСмыС мРНК (свободныС мРНП) (Spirin, 1964). Π­Ρ‚ΠΈ частицы Π±Ρ‹Π»ΠΈ Π½Π°Π·Π²Π°Π½Ρ‹ информосомами. Π—Π°Ρ‚Π΅ΠΌ Π±Ρ‹Π»ΠΈ ΠΏΠΎΠ»ΡƒΡ‡Π΅Π½Ρ‹ РНП, содСрТащиС гяРНК. Π­Ρ‚ΠΈ частицы ΠΏΠΎΠ»ΡƒΡ‡ΠΈΠ»ΠΈ Π½Π°Π·Π²Π°Π½ΠΈΠ΅ Π³Π΅Ρ‚Π΅Ρ€ΠΎΠ³Π΅Π½Π½Ρ‹Π΅ ядСрныС РНП (гяРНП) (Samarina et al., 1966). НаконСц, Π² 1968 Π³. Π±Ρ‹Π»ΠΎ ΠΏΠΎΠΊΠ°Π·Π°Π½ΠΎ, Ρ‡Ρ‚ΠΎ транслируСмая мРНК, находящаяся Π² ΠΏΠΎΠ»ΠΈΡΠΎΠΌΠ°Ρ…, Ρ‚Π°ΠΊΠΆΠ΅ ассоциирована с Π±Π΅Π»ΠΊΠ°ΠΌΠΈ (Cartouzou et al., 1968; Henshaw, 1968; Perry and Kelley, 1968). Π­Ρ‚ΠΈ полисомныС мРНП ΠΌΠΎΠ³ΡƒΡ‚ Π±Ρ‹Ρ‚ΡŒ Π²Ρ‹Π΄Π΅Π»Π΅Π½Ρ‹ послС диссоциации рибосом Π½Π° ΡΡƒΠ±Ρ‡Π°ΡΡ‚ΠΈΡ†Ρ‹. гяРНП ΠΈ Ρ†ΠΈΡ‚оплазматичСскиС мРНП Π΄Π²ΡƒΡ… классов ΠΎΠ±Π»Π°Π΄Π°ΡŽΡ‚ Π±Π»ΠΈΠ·ΠΊΠΈΠΌΠΈ Ρ„ΠΈΠ·ΠΈΠΊΠΎ-химичСскими свойствами, ΠΏΠΎΠ·Π²ΠΎΠ»ΡΡŽΡ‰ΠΈΠΌΠΈ ΠΎΠ±ΡŠΠ΅Π΄ΠΈΠ½ΠΈΡ‚ΡŒ ΠΈΡ… Π² ΠΎΠ΄ΠΈΠ½ Ρ‚ΠΈΠΏ частиц. А. Π‘. Π‘ΠΏΠΈΡ€ΠΈΠ½ ΠΏΡ€Π΅Π΄Π»ΠΎΠΆΠΈΠ» ΠΈΡΠΏΠΎΠ»ΡŒΠ·ΠΎΠ²Π°Ρ‚ΡŒ для этого Ρ‚ΠΈΠΏΠ° частиц Ρ‚Π΅Ρ€ΠΌΠΈΠ½ информосомы (Spirin, 1964; Spirin, 1969). Богласно этой Ρ‚Π΅Ρ€ΠΌΠΈΠ½ΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΌΠΎΠΆΠ½ΠΎ Ρ€Π°Π·Π»ΠΈΡ‡Π°Ρ‚ΡŒ Ρ‚Ρ€ΠΈ класса информосом: ядСрныС, свободныС цитоплазматичСскиС ΠΈ ΠΏΠΎΠ»ΠΈΡΠΎΠΌΠ½Ρ‹Π΅ транслируСмыС. Благодаря ΠΈΡ… ΡƒΠ½ΠΈΠΊΠ°Π»ΡŒΠ½Ρ‹ΠΌ свойствам, эти частицы ΠΌΠΎΠΆΠ½ΠΎ Π»Π΅Π³ΠΊΠΎ ΠΎΡ‚Π»ΠΈΡ‡ΠΈΡ‚ΡŒ ΠΎΡ‚ Π΄Ρ€ΡƒΠ³ΠΈΡ… Ρ‚ΠΈΠΏΠΎΠ² ΠΊΠ»Π΅Ρ‚ΠΎΡ‡Π½Ρ‹Ρ… РНП. НиТС пСрСчислСнны основныС характСристики информосом (Preobrazhensky and Spirin, 1978).

1) Π˜Π½Ρ„ΠΎΡ€ΠΌΠΎΡΠΎΠΌΡ‹ Ρ…Π°Ρ€Π°ΠΊΡ‚Π΅Ρ€ΠΈΠ·ΡƒΡŽΡ‚ΡΡ ΡˆΠΈΡ€ΠΎΠΊΠΈΠΌ сСдимСнтационным распрСдСлСниСм, ΠΎΡ‚Ρ€Π°ΠΆΠ°ΡŽΡ‰ΠΈΠΌ Π³Π΅Ρ‚Π΅Ρ€ΠΎΠ³Π΅Π½Π½ΠΎΡΡ‚ΡŒ мРНК ΠΈ Π΅Π΅ ΠΏΡ€Π΅Π΄ΡˆΠ΅ΡΡ‚Π²Π΅Π½Π½ΠΈΠΊΠΎΠ² ΠΏΠΎ Ρ€Π°Π·ΠΌΠ΅Ρ€Π°ΠΌ Π² Π±ΠΎΠ»ΡŒΡˆΠΈΠ½ΡΡ‚Π²Π΅ клСтоксущСствуСт линСйная коррСляция ΠΌΠ΅ΠΆΠ΄Ρƒ коэффициСнтом сСдимСнтации частиц ΠΈ Π ΠΠš, ΠΏΡ€ΠΈΡ‡Π΅ΠΌ коэффициСнты сСдимСнтации РНП ΠΏΡ€Π΅Π²Ρ‹ΡˆΠ°ΡŽΡ‚ коэффициСнт сСдимСнтации РНК Π² 2,5 — 3 Ρ€Π°Π·Π°.

2) ВсС Ρ‚Ρ€ΠΈ класса информосом ΠΈΠΌΠ΅ΡŽΡ‚ высокоС вСсовоС ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΠ΅ Π±Π΅Π»ΠΎΠΊ/РНК, Ρ€Π°Π²Π½ΠΎΠ΅ 3 для ядСрных ΠΈ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½Ρ‹Ρ… цитоплазматичСских РНП ΠΈ 2 для полисомныхэто обуславливаСт ΡƒΠ½ΠΈΠΊΠ°Π»ΡŒΠ½ΡƒΡŽ ΠΏΠ»Π°Π²ΡƒΡ‡ΡƒΡŽ ΠΏΠ»ΠΎΡ‚Π½ΠΎΡΡ‚ΡŒ Π² CsCl, Ρ€Π°Π²Π½ΡƒΡŽ 1,39 -1,4 Π³/см3 для ядСрных ΠΈ ΡΠ²ΠΎΠ±ΠΎΠ΄Π½Ρ‹Ρ… цитоплазматичСских РНП ΠΈ 1,45 Π³/см3 для полисомных транслируСмых мРНП.

3) РНК информосом ΠΎΠ±Π»Π°Π΄Π°Π΅Ρ‚ Ρ‡Ρ€Π΅Π·Π²Ρ‹Ρ‡Π°ΠΉΠ½ΠΎ высокой Ρ‡ΡƒΠ²ΡΡ‚Π²ΠΈΡ‚Π΅Π»ΡŒΠ½ΠΎΡΡ‚ΡŒΡŽ ΠΊ ΡΠ½Π΄ΠΎΡ€ΠΈΠ±ΠΎΠ½ΡƒΠΊΠ»Π΅Π°Π·Π°ΠΌ, Ρ‡Ρ‚ΠΎ ΡΠ²ΠΈΠ΄Π΅Ρ‚Π΅Π»ΡŒΡΡ‚Π²ΡƒΠ΅Ρ‚ ΠΎ Π΅Π΅ ΠΏΠΎΠ²Π΅Ρ€Ρ…ностном располоТСнии Π² Ρ‡Π°ΡΡ‚ΠΈΡ†Π°Ρ….

НСсмотря Π½Π° ΡΡ…одство основных Ρ„ΠΈΠ·ΠΈΠΊΠΎ-химичСских свойств информосом Ρ‚Ρ€Π΅Ρ… классов, Π½Π°Π±ΠΎΡ€ Π±Π΅Π»ΠΊΠΎΠ² Π² ΡΡ‚ΠΈΡ… частицах сущСствСнно различаСтся, ΠΏΠΎΡΠΊΠΎΠ»ΡŒΠΊΡƒ Ρ€Π°Π·Π»ΠΈΡ‡Π°ΡŽΡ‚ΡΡ Ρ‚Π΅ Ρ„ΡƒΠ½ΠΊΡ†ΠΈΠΈ, ΠΊΠΎΡ‚ΠΎΡ€Ρ‹Π΅ Π²Ρ‹ΠΏΠΎΠ»Π½ΡΡŽΡ‚ эти Π±Π΅Π»ΠΊΠΈ. Π‘Π΅Π»ΠΊΠΈ гяРНП ΠΏΡ€ΠΈΠ½ΠΈΠΌΠ°ΡŽΡ‚ участиС Π² ΡΠΈΠ½Ρ‚Π΅Π·Π΅ ΠΏΡ€Π΅Π΄ΡˆΠ΅ΡΡ‚Π²Π΅Π½Π½ΠΈΠΊΠΎΠ² мРНК ΠΈ ΠΈΡ… ΠΏΡ€ΠΎΡ†Π΅ΡΡΠΈΠ½Π³Π΅ Π΄ΠΎ Π·Ρ€Π΅Π»Ρ‹Ρ… мРНК, Π²ΠΊΠ»ΡŽΡ‡Π°Ρ кэпированиС 5' ΠΊΠΎΠ½Ρ†Π°, ΡƒΠΊΠΎΡ€Π°Ρ‡ΠΈΠ²Π°Π½ΠΈΠ΅ 3' ΠΊΠΎΠ½Ρ†Π° ΠΈ Π΅Π³ΠΎ ΠΏΠΎΡΠ»Π΅Π΄ΡƒΡŽΡ‰Π΅Π΅ ΠΏΠΎΠ»ΠΈΠ°Π΄Π΅Π½ΠΈΠ»ΠΈΡ€ΠΎΠ²Π°Π½ΠΈΠ΅ ΠΈ, Π½Π°ΠΊΠΎΠ½Π΅Ρ†, Π²Ρ‹Ρ€Π΅Π·Π°Π½ΠΈΠ΅ ΠΈΠ½Ρ‚Ρ€ΠΎΠ½ΠΎΠ² ΠΈ ΡΠΎΠ΅Π΄ΠΈΠ½Π΅Π½ΠΈΠ΅ экзонов Π² ΠΏΡ€ΠΎΡ†Π΅ΡΡΠ΅, ΠΏΠΎΠ»ΡƒΡ‡ΠΈΠ²ΡˆΠ΅ΠΌ Π½Π°Π·Π²Π°Π½ΠΈΠ΅ сплайсинг. Π‘Π΅Π»ΠΊΠΈ гяРНП Ρ‚Π°ΠΊΠΆΠ΅ ΡƒΡ‡Π°ΡΡ‚Π²ΡƒΡŽΡ‚ Π² Ρ‚ранспортС мРНК ΠΈΠ· ΡΠ΄Ρ€Π° Π² Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡƒ Ρ‡Π΅Ρ€Π΅Π· ядСрныС ΠΏΠΎΡ€Ρ‹. Π‘Π΅Π»ΠΊΠΈ цитоплазматичСских мРНП Ρ€Π΅Π³ΡƒΠ»ΠΈΡ€ΡƒΡŽΡ‚ Ρ‚Ρ€Π°Π½ΡΠ»ΡΡ†ΠΈΡŽ, ΠΎΠΏΡ€Π΅Π΄Π΅Π»ΡΡŽΡ‚ врСмя ΠΆΠΈΠ·Π½ΠΈ ΠΈΠ½Π΄ΠΈΠ²ΠΈΠ΄ΡƒΠ°Π»ΡŒΠ½Ρ‹Ρ… ΠΌΠΎΠ»Π΅ΠΊΡƒΠ» мРНК ΠΈ ΠΈΡ… Π»ΠΎΠΊΠ°Π»ΠΈΠ·Π°Ρ†ΠΈΡŽ Π² ΠΎΠΏΡ€Π΅Π΄Π΅Π»Π΅Π½Π½Ρ‹Ρ… мСстах Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡ‹. Π’Π°ΠΊΠΈΠΌ ΠΎΠ±Ρ€Π°Π·ΠΎΠΌ, мРНК ΠΏΡ€ΠΈ транспортС ΠΈΠ· ΡΠ΄Ρ€Π° Π² Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡƒ ΠΈ ΠΏΠ΅Ρ€Π΅Ρ…ΠΎΠ΄Π΅ Π² ΠΏΠΎΠ»ΠΈΡΠΎΠΌΡ‹ Π² Π·Π½Π°Ρ‡ΠΈΡ‚Π΅Π»ΡŒΠ½ΠΎΠΉ стСпСни «ΠΏΠ΅Ρ€Π΅ΠΎΠ΄Π΅Π²Π°ΡŽΡ‚ΡΡ». ВмСстС с Ρ‚Π΅ΠΌ, Π½Π΅ΠΊΠΎΡ‚ΠΎΡ€Ρ‹Π΅ Π±Π΅Π»ΠΊΠΈ, ассоциированныС с ΠΌΠ ΠΠš Π² ΡΠ΄Ρ€Π΅, выходят вмСстС с Π½Π΅ΠΉ Π² Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡƒ ΠΈ ΠΏΠΎΡ‚ΠΎΠΌ снова Π²ΠΎΠ·Π²Ρ€Π°Ρ‰Π°ΡŽΡ‚ΡΡ Π² ΡΠ΄Ρ€ΠΎ. Π’Π°ΠΊΠΈΠ΅ Π±Π΅Π»ΠΊΠΈ ΠΏΠΎΠ»ΡƒΡ‡ΠΈΠ»ΠΈ Π½Π°Π·Π²Π°Π½ΠΈΠ΅ Ρ‡Π΅Π»Π½ΠΎΡ‡Π½Ρ‹Ρ… Π±Π΅Π»ΠΊΠΎΠ².

ΠœΠ½ΠΎΠ³ΠΎΡ‡ΠΈΡΠ»Π΅Π½Π½Ρ‹Π΅ Π±Π΅Π»ΠΊΠΈ, входящиС Π² ΡΠΎΡΡ‚Π°Π² информосом, ΠΌΠΎΠΆΠ½ΠΎ условно ΠΏΠΎΠ΄Ρ€Π°Π·Π΄Π΅Π»ΠΈΡ‚ΡŒ Π½Π° Ρ‚Ρ€ΠΈ Π³Ρ€ΡƒΠΏΠΏΡ‹. ΠŸΠ΅Ρ€Π²ΡƒΡŽ Π³Ρ€ΡƒΠΏΠΏΡƒ ΡΠΎΡΡ‚Π°Π²Π»ΡΡŽΡ‚ Π±Π΅Π»ΠΊΠΈ, спСцифичСски ΡΠ²ΡΠ·Ρ‹Π²Π°ΡŽΡ‰ΠΈΠ΅ΡΡ Ρ‚ΠΎΠ»ΡŒΠΊΠΎ с Π½Π΅ΠΊΠΎΡ‚ΠΎΡ€Ρ‹ΠΌΠΈ мРНК, ΠΈΠΌΠ΅ΡŽΡ‰ΠΈΠΌΠΈ участки узнавания для этих Π±Π΅Π»ΠΊΠΎΠ², Π½Π°ΠΏΡ€ΠΈΠΌΠ΅Ρ€, Π±Π΅Π»ΠΊΠΈ, ΡƒΡ‡Π°ΡΡ‚Π²ΡƒΡŽΡ‰ΠΈΠ΅ Π² ΡΠ΅Π»Π΅ΠΊΡ‚ΠΈΠ²Π½ΠΎΠΉ рСгуляции активности ΠΈ ΡΡ‚Π°Π±ΠΈΠ»ΡŒΠ½ΠΎΡΡ‚ΠΈ мРНК, Π° Ρ‚Π°ΠΊΠΆΠ΅ ΠΎΠΏΡ€Π΅Π΄Π΅Π»ΡΡŽΡ‰ΠΈΠ΅ ΡΠΏΠ΅Ρ†ΠΈΡ„ΠΈΡ‡Π΅ΡΠΊΡƒΡŽ Π»ΠΎΠΊΠ°Π»ΠΈΠ·Π°Ρ†ΠΈΡŽ мРНК Π² ΠΊΠ»Π΅Ρ‚ΠΊΠ΅. Ко Π²Ρ‚ΠΎΡ€ΠΎΠΉ Π³Ρ€ΡƒΠΏΠΏΠ΅ ΠΌΠΎΠΆΠ½ΠΎ отнСсти Π±Π΅Π»ΠΊΠΈ, ΠΏΡ€ΠΈΡΡƒΡ‚ΡΡ‚Π²ΡƒΡŽΡ‰ΠΈΠ΅ Π½Π° Π²ΡΠ΅Ρ… ΠΈΠ»ΠΈ Π±ΠΎΠ»ΡŒΡˆΠΈΠ½ΡΡ‚Π²Π΅ мРНК, Π½ΠΎ Π² Π΅Π΄ΠΈΠ½ΠΈΡ‡Π½Ρ‹Ρ… копиях ΠΈ ΠΎΠ³Ρ€Π°Π½ΠΈΡ‡Π΅Π½Π½ΠΎΠ΅ врСмя, Π½Π°ΠΏΡ€ΠΈΠΌΠ΅Ρ€ Ρ„Π΅Ρ€ΠΌΠ΅Π½Ρ‚Ρ‹, ΡƒΡ‡Π°ΡΡ‚Π²ΡƒΡŽΡ‰ΠΈΠ΅ Π² ΠΏΡ€ΠΎΡ†Π΅ΡΡΠΈΠ½Π³Π΅ мРНК, Ρ„Π°ΠΊΡ‚ΠΎΡ€Ρ‹ трансляции. Π’ Ρ‚Ρ€Π΅Ρ‚ΡŒΡŽ Π³Ρ€ΡƒΠΏΠΏΡƒ входят Π±Π΅Π»ΠΊΠΈ, ассоциированныС с Π±ΠΎΠ»ΡŒΡˆΠΈΠ½ΡΡ‚Π²ΠΎΠΌ ΠΈΠ»ΠΈ всСми мРНК ΠΈ ΠΏΡ€Π΅Π΄ΡΡ‚Π°Π²Π»Π΅Π½Π½Ρ‹Π΅ Π½Π° Π½ΠΈΡ… Π² Π±ΠΎΠ»ΡŒΡˆΠΎΠΌ количСствС ΠΊΠΎΠΏΠΈΠΉ. ИмСнно эти Π±Π΅Π»ΠΊΠΈ ΠΎΠ±Π½Π°Ρ€ΡƒΠΆΠΈΠ²Π°ΡŽΡ‚ΡΡ ΠΊΠ°ΠΊ ΠΌΠ°ΠΆΠΎΡ€Ρ‹ Π² ΡΡƒΠΌΠΌΠ°Ρ€Π½Ρ‹Ρ… ΠΏΡ€Π΅ΠΏΠ°Ρ€Π°Ρ‚Π°Ρ… Π±Π΅Π»ΠΊΠΎΠ² информосом ядра ΠΈ Ρ†ΠΈΡ‚ΠΎΠΏΠ»Π°Π·ΠΌΡ‹. Они Π²Ρ‹ΡΠ²Π»ΡΡŽΡ‚ΡΡ Π² ΠΏΡ€Π΅ΠΏΠ°Ρ€Π°Ρ‚Π°Ρ… информосом ΠΈΠ· Ρ€Π°Π·Π½Ρ‹Ρ… ΠΊΠ»Π΅Ρ‚ΠΎΠΊ ΠΈ Ρ‚ΠΊΠ°Π½Π΅ΠΉ ΠΎΡ€Π³Π°Π½ΠΈΠ·ΠΌΠ° ΠΈ, скорСС всСго, ΠΎΠΏΡ€Π΅Π΄Π΅Π»ΡΡŽΡ‚ ΡƒΠ½ΠΈΠΊΠ°Π»ΡŒΠ½Ρ‹Π΅ Ρ„ΠΈΠ·ΠΈΠΊΠΎ-химичСскиС свойства информосом. Π‘Ρ€Π΅Π΄ΠΈ ΠΌΠ°ΠΆΠΎΡ€Π½Ρ‹Ρ… Π±Π΅Π»ΠΊΠΎΠ² ядСрных информосом Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ Ρ…ΠΎΡ€ΠΎΡˆΠΎ ΠΈΠ·ΡƒΡ‡Π΅Π½Ρ‹ Π±Π΅Π»ΠΊΠΈ А1/Π’2, А2/Π’1 ΠΈ Π‘1/Π‘2, Π° ΡΡ€Π΅Π΄ΠΈ цитоплазматичСских мРНП — Ρ€50 ΠΈ ΠΏΠΎΠ»ΠΈ (А)-ΡΠ²ΡΠ·Ρ‹Π²Π°ΡŽΡ‰ΠΈΠΉ Π±Π΅Π»ΠΎΠΊ РАВР (goly (A) binding protein). Π‘Π΅Π»ΠΊΠΈ ΠΏΠ΅Ρ€Π²ΠΎΠΉ ΠΈ Π²Ρ‚ΠΎΡ€ΠΎΠΉ Π³Ρ€ΡƒΠΏΠΏΡ‹, Π½Π°ΠΏΡ€ΠΎΡ‚ΠΈΠ², прСдставлСны многочислСнными ΠΌΠΈΠ½ΠΎΡ€Π°ΠΌΠΈ Π² ΡΡƒΠΌΠΌΠ°Ρ€Π½Ρ‹Ρ… ΠΏΡ€Π΅ΠΏΠ°Ρ€Π°Ρ‚Π°Ρ… информосом, ΠΈ ΠΈΡ… Π½Π°Π±ΠΎΡ€ ΠΌΠΎΠΆΠ΅Ρ‚ сильно Π²Π°Ρ€ΡŒΠΈΡ€ΠΎΠ²Π°Ρ‚ΡŒ Π² Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡ‚ΠΈ ΠΎΡ‚ ΠΈΡΡ‚ΠΎΡ‡Π½ΠΈΠΊΠ° получСния.

Описанию строСния ΠΈ Ρ„ункционирования ΠΌΠΈΠ½ΠΎΡ€Π½Ρ‹Ρ… Π±Π΅Π»ΠΊΠΎΠ² ядСрных ΠΈ Ρ†ΠΈΡ‚оплазматичСских мРНП посвящСно мноТСство ΠΎΠ±Π·ΠΎΡ€Π½Ρ‹Ρ… статСй, рСгулярно ΠΏΠΎΡΠ²Π»ΡΡŽΡ‰ΠΈΡ…ΡΡ ΠΊΠ°ΠΊ Π² ΠΎΡ‚СчСствСнной, Ρ‚Π°ΠΊ ΠΈ Π² Π·Π°Ρ€ΡƒΠ±Π΅ΠΆΠ½ΠΎΠΉ Π»ΠΈΡ‚Π΅Ρ€Π°Ρ‚ΡƒΡ€Π΅. К ΡΠΎΠΆΠ°Π»Π΅Π½ΠΈΡŽ, Ρ€Π°ΡΡΠΌΠΎΡ‚Ρ€Π΅Π½ΠΈΡŽ ΠΌΠ°ΠΆΠΎΡ€Π½Ρ‹Ρ… Π±Π΅Π»ΠΊΠΎΠ² Π±Ρ‹Π»ΠΎ ΡƒΠ΄Π΅Π»Π΅Π½ΠΎ Π³ΠΎΡ€Π°Π·Π΄ΠΎ мСньшС внимания Π² ΠΎΠ±Π·ΠΎΡ€Π½ΠΎΠΉ Π»ΠΈΡ‚Π΅Ρ€Π°Ρ‚ΡƒΡ€Π΅, нСсмотря Π½Π° Ρ€Π°ΡΡ‚ΡƒΡ‰Π΅Π΅ Π΅ΠΆΠ΅Π³ΠΎΠ΄Π½ΠΎ количСство Π½ΠΎΠ²Ρ‹Ρ… Π΄Π°Π½Π½Ρ‹Ρ…, ΠΊΠ°ΡΠ°ΡŽΡ‰ΠΈΡ…ΡΡ ΠΈΡ… ΡΡ‚роСния ΠΈ Ρ„ункционирования. Π’ ΡΠ²ΡΠ·ΠΈ с ΡΡ‚ΠΈΠΌ Π½Π°ΠΌ показалось ΠΎΡ‡Π΅Π½ΡŒ Π²Π°ΠΆΠ½Ρ‹ΠΌ ΠΈ ΠΈΠ½Ρ‚СрСсным ΠΏΡ€ΠΎΠ°Π½Π°Π»ΠΈΠ·ΠΈΡ€ΠΎΠ²Π°Ρ‚ΡŒ ΠΊΠ°ΠΊ Π½Π΅Π΄Π°Π²Π½ΠΈΠ΅, Ρ‚Π°ΠΊ ΠΈ Ρ€Π°Π½Π΅Π΅ ΠΏΠΎΠ»ΡƒΡ‡Π΅Π½Π½Ρ‹Π΅ Ρ€Π΅Π·ΡƒΠ»ΡŒΡ‚Π°Ρ‚Ρ‹ ΠΏΠΎ ΡΡ‚ΠΎΠΉ Ρ‚Π΅ΠΌΠ΅ Π² ΠΏΡ€Π΅Π΄ΡΡ‚Π°Π²Π»Π΅Π½Π½ΠΎΠΌ здСсь ΠΎΠ±Π·ΠΎΡ€Π΅ Π»ΠΈΡ‚Π΅Ρ€Π°Ρ‚ΡƒΡ€Ρ‹, ΠΎΠ·Π°Π³Π»Π°Π²Π»Π΅Π½Π½ΠΎΠΌ «ΠœΠ°ΠΆΠΎΡ€Π½Ρ‹Π΅ Π±Π΅Π»ΠΊΠΈ ядСрных ΠΈ Ρ†ΠΈΡ‚оплазматичСских мРНП: строСниС ΠΈ Ρ„ΡƒΠ½ΠΊΡ†ΠΈΠΎΠ½ΠΈΡ€ΠΎΠ²Π°Π½ΠΈΠ΅».

ΠžΠ‘Π—ΠžΠ  Π›Π˜Π’Π•Π ΠΠ’Π£Π Π«.

ΠœΠΠ–ΠžΠ ΠΠ«Π• Π‘Π•Π›ΠšΠ˜ ЯДЕРНЫΠ₯ И Π¦Π˜Π’ΠžΠŸΠ›ΠΠ—ΠœΠΠ’Π˜Π§Π•Π‘ΠšΠ˜Π₯ мРНП: Π‘Π’Π ΠžΠ•ΠΠ˜Π• И Π€Π£ΠΠšΠ¦Π˜ΠžΠΠ˜Π ΠžΠ’ΠΠΠ˜Π•.

I. Π“Π΅Ρ‚Π΅Ρ€ΠΎΠ³Π΅Π½Π½Ρ‹Π΅ ядСрныС Ρ€ΠΈΠ±ΠΎΠ½ΡƒΠΊΠ»Π΅ΠΎΠΏΡ€ΠΎΡ‚Π΅ΠΈΠ΄Π½Ρ‹Π΅ частицы (гяРНП).

Π²Ρ‹Π²ΠΎΠ΄Ρ‹.

1. ΠŸΡ€ΠΈ насыщСнии 9S Π°-Π³Π»ΠΎΠ±ΠΈΠ½ΠΎΠ²ΠΎΠΉ мРНК ΠΌΠ°ΠΆΠΎΡ€Π½Ρ‹ΠΌ Π±Π΅Π»ΠΊΠΎΠΌ мРНП, Ρ€50, ΠΎΠ±Ρ€Π°Π·ΡƒΡŽΡ‚ΡΡ Π³ΠΎΠΌΠΎΠ³Π΅Π½Π½Ρ‹Π΅ частицы с ΠΊΠΎΡΡ„Ρ„ΠΈΡ†ΠΈΠ΅Π½Ρ‚ΠΎΠΌ сСдимСнтации ΠΎΠΊΠΎΠ»ΠΎ 28S, Ρ‡Ρ‚ΠΎ ΠΏΡ€ΠΈΠΌΠ΅Ρ€Π½ΠΎ соотвСтствуСт Π²Π΅Π»ΠΈΡ‡ΠΈΠ½Π΅ коэффициСнта сСдимСнтации ΠΏΡ€ΠΈΡ€ΠΎΠ΄Π½Ρ‹Ρ… мРНП (информосом) с ΠΌΠ ΠΠš использованного Ρ€Π°Π·ΠΌΠ΅Ρ€Π°.

2. Одного Π±Π΅Π»ΠΊΠ° Ρ€50 достаточно, для формирования с ΠΌΠ ΠΠš частиц с ΠΏΠ»Π°Π²ΡƒΡ‡Π΅ΠΉ ΠΏΠ»ΠΎΡ‚Π½ΠΎΡΡ‚ΡŒΡŽ Π² CsCl 1,4 Π³/см3, Ρ‡Ρ‚ΠΎ соотвСтствуСт Π²Π΅Π»ΠΈΡ‡ΠΈΠ½Π΅ ΠΏΠ»Π°Π²ΡƒΡ‡Π΅ΠΉ плотности основного плотностного ΠΊΠΎΠΌΠΏΠΎΠ½Π΅Π½Ρ‚Π° ΠΏΡ€ΠΈΡ€ΠΎΠ΄Π½Ρ‹Ρ… мРНП.

3. ΠŸΡ€ΠΈ Π½ΠΈΠ·ΠΊΠΎΠΌ ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΠΈ Ρ€50/мРНК исходно ΠΌΡƒΠ»ΡŒΡ‚ΠΈΠΌΠ΅Ρ€Π½Ρ‹ΠΉ Ρ€50 связываСтся с ΠΌΠ ΠΠš Π² Π²ΠΈΠ΄Π΅ ΠΌΠΎΠ½ΠΎΠΌΠ΅Ρ€Π°. ΠŸΡ€ΠΈ ΡƒΠ²Π΅Π»ΠΈΡ‡Π΅Π½ΠΈΠΈ ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡ Ρ€50/мРНК Ρ€50 ΠΎΠ±Ρ€Π°Π·ΡƒΠ΅Ρ‚ Π½Π° ΠΌΠ ΠΠš ΠΌΡƒΠ»ΡŒΡ‚ΠΈΠΌΠ΅Ρ€Ρ‹. По ΠΌΠ΅Ρ€Π΅ увСличСния ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡ Ρ€50/мРНК увСличиваСтся ΠΎΡ‚Π½ΠΎΡΠΈΡ‚Π΅Π»ΡŒΠ½Ρ‹ΠΉ ΠΊΠΎΠ½Ρ‚Π°ΠΊΡ‚ с Π ΠΠš N-ΠΊΠΎΠ½Ρ†Π΅Π²ΠΎΠΉ части ΠΌΠΎΠ»Π΅ΠΊΡƒΠ»Ρ‹ Ρ€50 с Π΄ΠΎΠΌΠ΅Π½ΠΎΠΌ Ρ…ΠΎΠ»ΠΎΠ΄ΠΎΠ²ΠΎΠ³ΠΎ шока ΠΈ ΡƒΠΌΠ΅Π½ΡŒΡˆΠ°Π΅Ρ‚ся ΠΎΡ‚Π½ΠΎΡΠΈΡ‚Π΅Π»ΡŒΠ½Ρ‹ΠΉ ΠΊΠΎΠ½Ρ‚Π°ΠΊΡ‚ с Π ΠΠš Π‘-ΠΊΠΎΠ½Ρ†Π΅Π²ΠΎΠ³ΠΎ Π΄ΠΎΠΌΠ΅Π½Π° Ρ€50.

4. Ρ€50 ускоряСт ΠΎΡ‚ΠΆΠΈΠ³ ΠΈ ΠΎΠ±ΠΌΠ΅Π½ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ РНК ΠΈ ΡΠΏΠΎΡΠΎΠ±ΡΡ‚Π²ΡƒΠ΅Ρ‚ ΠΎΠ±Ρ€Π°Π·ΠΎΠ²Π°Π½ΠΈΡŽ Π½Π°ΠΈΠ±ΠΎΠ»Π΅Π΅ протяТСнных ΠΈ ΡΠΎΠ²Π΅Ρ€ΡˆΠ΅Π½Π½Ρ‹Ρ… дуплСксов.

5. Π’ Π·Π°Π²ΠΈΡΠΈΠΌΠΎΡΡ‚ΠΈ ΠΎΡ‚ ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡ Ρ€50/РНК Ρ€50 ΠΌΠΎΠΆΠ΅Ρ‚ Π²Ρ‹Π·Ρ‹Π²Π°Ρ‚ΡŒ ΠΎΡ‚ΠΆΠΈΠ³ Π΄Π²ΠΎΠΉΠ½Ρ‹Ρ… спиралСй РНК (ΠΏΡ€ΠΈ Π½ΠΈΠ·ΠΊΠΈΡ… ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡΡ… Ρ€50/мРНК) ΠΈΠ»ΠΈ, Π½Π°ΠΎΠ±ΠΎΡ€ΠΎΡ‚, ΠΈΡ… ΠΏΠ»Π°Π²Π»Π΅Π½ΠΈΠ΅ (ΠΏΡ€ΠΈ высоких значСниях этого ΡΠΎΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΡ).

6. Ρ€50 Π²Ρ‹Π·Ρ‹Π²Π°Π΅Ρ‚ ΠΎΡ‚ΠΆΠΈΠ³ ΠΊΠΎΠΌΠΏΠ»Π΅ΠΌΠ΅Π½Ρ‚Π°Ρ€Π½Ρ‹Ρ… Ρ†Π΅ΠΏΠ΅ΠΉ Π”ΠΠš, ΠΈ ΡΡ‚Π° Π°ΠΊΡ‚ΠΈΠ²Π½ΠΎΡΡ‚ΡŒ Π±Π΅Π»ΠΊΠ° ингибируСтся фосорилированиСм Π΅Π³ΠΎ ΠΊΠ°Π·Π΅ΠΈΠ½ΠΊΠΈΠ½Π°Π·ΠΎΠΉ II.

Π‘Π›ΠΠ“ΠžΠ”ΠΠ ΠΠžΠ‘Π’Π˜.

Π”ΠΎΠ»ΠΆΠ΅Π½ ΠΏΡ€ΠΈΠ·Π½Π°Ρ‚ΡŒΡΡ, Ρ‡Ρ‚ΠΎ эта Π³Π»Π°Π²Π° самая приятная для написания ΠΈ Π½Π΅ Ρ‚ΠΎΠ»ΡŒΠΊΠΎ ΠΏΠΎΡ‚ΠΎΠΌΡƒ, Ρ‡Ρ‚ΠΎ послСдняя. Π—Π΄Π΅ΡΡŒ я ΠΌΠΎΠ³Ρƒ ΠΏΠΎΠ±Π»Π°Π³ΠΎΠ΄Π°Ρ€ΠΈΡ‚ΡŒ Ρ‚Π΅Ρ… людСй, ΠΊΡ‚ΠΎ ΠΏΠΎΠΌΠΎΠ³ ΠΌΠ½Π΅ ΡΠ΄Π΅Π»Π°Ρ‚ΡŒ эту Ρ€Π°Π±ΠΎΡ‚Ρƒ, ΠΊΡ‚ΠΎ воспитывал мСня, ΠΊΠ°ΠΊ Π½Π°ΡƒΡ‡Π½ΠΎΠ³ΠΎ сотрудника, всСх Ρ‚Π΅Ρ…, ΠΊΡ‚ΠΎ создавал ΠΏΡ€ΠΈΡΡ‚Π½ΡƒΡŽ Ρ‚Π²ΠΎΡ€Ρ‡Π΅ΡΠΊΡƒΡŽ атмосфСру.

ΠŸΡ€Π΅ΠΆΠ΄Π΅ всСго, я Π³Π»ΡƒΠ±ΠΎΠΊΠΎ Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€Π΅Π½ ΠΌΠΎΠ΅ΠΌΡƒ Π½Π°ΡƒΡ‡Π½ΠΎΠΌΡƒ Ρ€ΡƒΠΊΠΎΠ²ΠΎΠ΄ΠΈΡ‚Π΅Π»ΡŽ Π›ΡŒΠ²Ρƒ ΠŸΠ°Π²Π»ΠΎΠ²ΠΈΡ‡Ρƒ ΠžΠ²Ρ‡ΠΈΠ½Π½ΠΈΠΊΠΎΠ²Ρƒ. Он Π²Π·ΡΠ» мСня Π² ΡΠ²ΠΎΡŽ Π»Π°Π±ΠΎΡ€Π°Ρ‚ΠΎΡ€ΠΈΡŽ Π΅Ρ‰Π΅ ΡΠΎΠ²Π΅Ρ€ΡˆΠ΅Π½Π½ΠΎ Π½Π΅ΠΎΠ±ΡƒΡ‡Π΅Π½Π½Ρ‹ΠΌ ΠΈ «Π·Π΅Π»Π΅Π½Ρ‹ΠΌ». Π’ Ρ‚ΠΎΠΌ, Ρ‡Ρ‚ΠΎ я ΡΠ΅Π³ΠΎΠ΄Π½Ρ собой ΠΏΡ€Π΅Π΄ΡΡ‚Π°Π²Π»ΡΡŽ, ΠΊΠ°ΠΊ Π½Π°ΡƒΡ‡Π½Ρ‹ΠΉ Ρ€Π°Π±ΠΎΡ‚Π½ΠΈΠΊ, огромная Π΅Π³ΠΎ заслуга. Он ΠΏΡ€ΠΈΡΡ‚Π°Π»ΡŒΠ½ΠΎ ΠΈ Π²Π½ΠΈΠΌΠ°Ρ‚Π΅Π»ΡŒΠ½ΠΎ Ρ€ΡƒΠΊΠΎΠ²ΠΎΠ΄ΠΈΠ» ΠΊΠ°ΠΆΠ΄Ρ‹ΠΌ этапом ΠΌΠΎΠ΅ΠΉ ΠΈΡΡΠ»Π΅Π΄ΠΎΠ²Π°Ρ‚Π΅Π»ΡŒΡΠΊΠΎΠΉ Ρ€Π°Π±ΠΎΡ‚Ρ‹. НСоцСним Π΅Π³ΠΎ Π²ΠΊΠ»Π°Π΄ ΠΈ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ тСкста диссСртации. ОсобСнно я Ρ…ΠΎΡ‡Ρƒ Π΅Π³ΠΎ ΠΏΠΎΠ±Π»Π°Π³ΠΎΠ΄Π°Ρ€ΠΈΡ‚ΡŒ Π·Π° ΡΠΎΠ·Π΄Π°Π½ΠΈΠ΅ ΡƒΠ½ΠΈΠΊΠ°Π»ΡŒΠ½ΠΎΠΉ творчСской ΠΈ Ρ€Π°Π±ΠΎΡ‡Π΅ΠΉ атмосфСры Π² Π»Π°Π±ΠΎΡ€Π°Ρ‚ΠΎΡ€ΠΈΠΈ ΠΈ Π·Π° Π²Ρ‹Π±ΠΎΡ€ Π² ΡΠ²ΠΎΠ΅ врСмя интСрСсной Π½Π°ΡƒΡ‡Π½ΠΎΠΉ Ρ‚Π΅ΠΌΡ‹ — ΠΈΠ·ΡƒΡ‡Π΅Π½ΠΈΠ΅ Π±Π΅Π»ΠΊΠ° Ρ€50.

Π― ΠΈΡΠΊΡ€Π΅Π½Π½Π΅ Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€Π΅Π½ Π’Π°Π»Π΅Π½Ρ‚ΠΈΠ½Ρƒ Устинову, ΠΊΠΎΡ‚ΠΎΡ€Ρ‹ΠΉ ΠΎΠ±ΡƒΡ‡ΠΈΠ» мСня мноТСству ΠΌΠ΅Ρ‚ΠΎΠ΄ΠΎΠ² молСкулярной Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΠΈ ΠΈ Π±ΠΈΠΎΡ…ΠΈΠΌΠΈΠΈ ΠΈ ΠΊΠΎΡ‚ΠΎΡ€Ρ‹ΠΉ воспитал Π²ΠΎ ΠΌΠ½Π΅ Π°ΠΊΠΊΡƒΡ€Π°Ρ‚Π½ΠΎΡΡ‚ΡŒ Π½Π΅ Ρ‚ΠΎΠ»ΡŒΠΊΠΎ Π² ΠΏΠΎΡΡ‚Π°Π½ΠΎΠ²ΠΊΠ΅ экспСримСнтов, Π½ΠΎ ΠΈ Π² ΠΏΠΎΠ΄Π΄Π΅Ρ€ΠΆΠ°Π½ΠΈΠΈ порядка Π½Π° Ρ€Π°Π±ΠΎΡ‡Π΅ΠΌ столС.

Π― ΠΈΡΠΊΠ»ΡŽΡ‡ΠΈΡ‚Π΅Π»ΡŒΠ½ΠΎ ΠΏΡ€ΠΈΠ·Π½Π°Ρ‚Π΅Π»Π΅Π½ ОлС Π‘ΠΊΠ°Π±ΠΊΠΈΠ½ΠΎΠΉ Π·Π° ΠΏΠΎΡΡ‚оянноС Π΅Π΅ Π²Π½ΠΈΠΌΠ°Π½ΠΈΠ΅ ΠΊ ΠΌΠΎΠ΅ΠΉ Ρ€Π°Π±ΠΎΡ‚Π΅ ΠΈ Π·Π° Π±Π΅ΡΠΊΠΎΠ½Π΅Ρ‡Π½ΠΎΠ΅ количСство ΠΊΠΎΠ½ΡΡƒΠ»ΡŒΡ‚Π°Ρ†ΠΈΠΉ, ΠΊΠΎΡ‚ΠΎΡ€Ρ‹Π΅ ΠΎΠ½Π° ΠΌΠ½Π΅ бСскорыстно Π΄Π°Π²Π°Π»Π° Π½Π΅ Ρ‚ΠΎΠ»ΡŒΠΊΠΎ Π½Π° Ρ€Π°Π±ΠΎΡ‚Π΅, Π½ΠΎ ΠΈ Π΄ΠΎΠΌΠ°. Π’Π°ΠΊΠΆΠ΅ я Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€ΡŽ Π΅Π΅ Π·Π° Ρ‚Ρƒ ΠΎΠ³Ρ€ΠΎΠΌΠ½ΡƒΡŽ ΠΏΠΎΠ΄Π΄Π΅Ρ€ΠΆΠΊΡƒ, ΠΊΠΎΡ‚ΠΎΡ€ΡƒΡŽ ΠΎΠ½Π° ΠΌΠ½Π΅ всСгда ΠΎΠΊΠ°Π·Ρ‹Π²Π°Π»Π°, особСнно Π² Ρ‚Ρ€ΡƒΠ΄Π½Ρ‹Π΅ для мСня ΠΌΠΎΠΌΠ΅Π½Ρ‚Ρ‹.

Π― ΠΎΡ‡Π΅Π½ΡŒ Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€Π΅Π½ Π’Π°Π»Π΅Π½Ρ‚ΠΈΠ½Π΅ Π•Π²Π΄ΠΎΠΊΠΈΠΌΠΎΠ²ΠΎΠΉ Π·Π° Ρ‚ΠΎ, Ρ‡Ρ‚ΠΎ ΠΎΠ½Π° Π½Π°ΡƒΡ‡ΠΈΠ»Π° мСня «ΠΌΠ½ΠΎΠ³ΠΎ Π΄ΡƒΠΌΠ°Ρ‚ΡŒ» ΠΏΡ€Π΅ΠΆΠ΄Π΅, Ρ‡Π΅ΠΌ Π½Π°Ρ‡ΠΈΠ½Π°Ρ‚ΡŒ «ΠΌΠ½ΠΎΠ³ΠΎ ΠΊΠ°ΠΏΠ°Ρ‚ΡŒ». ΠšΡ€ΠΎΠΌΠ΅ Ρ‚ΠΎΠ³ΠΎ, я Ρ‚Π°ΠΊΠΆΠ΅ Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€ΡŽ Π΅Π΅ Π·Π° ΠΎΠ±ΡƒΡ‡Π΅Π½ΠΈΠ΅ мСня ΠΌΠ½ΠΎΠ³ΠΈΠΌ ΠΌΠ΅Ρ‚ΠΎΠ΄Π°ΠΌ Π±ΠΈΠΎΡ…ΠΈΠΌΠΈΠΈ ΠΈ ΠΌΠΎΠ»Π΅ΠΊΡƒΠ»ΡΡ€Π½ΠΎΠΉ Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΠΈ.

Π’ ΡΡ‚ΠΎΠΉ Ρ€Π°Π±ΠΎΡ‚Π΅ Π΅ΡΡ‚ΡŒ большой Π²ΠΊΠ»Π°Π΄ ΠΌΠΎΠΈΡ… ΠΊΠΎΠ»Π»Π΅Π³ — АлСксСя Π‘ΠΎΡ€ΠΎΠΊΠΈΠ½Π° ΠΈ ΠšΠΎΠ½ΡΡ‚Π°Π½Ρ‚ΠΈΠ½Π° Π§Π΅Ρ€Π½ΠΎΠ²Π°. Они ΠΏΠΎΠΌΠΎΠ³Π°Π»ΠΈ ΠΌΠ½Π΅ ΠΏΡ€ΠΈ Π²Ρ‹ΠΏΠΎΠ»Π½Π΅Π½ΠΈΠΈ ΠΌΠ½ΠΎΠ³ΠΈΡ… экспСримСнтов ΠΈ ΠΈΠΌ я ΠΎΡ‡Π΅Π½ΡŒ ΠΏΡ€ΠΈΠ·Π½Π°Ρ‚Π΅Π»Π΅Π½.

ΠžΡ‚Π΄Π΅Π»ΡŒΠ½ΠΎΠ΅ большоС спасибо Π•Π»Π΅Π½Π΅ Π‘ΠΎΠ±ΠΎΠ»Π΅Π²ΠΎΠΉ ΠΈ Π•Π»Π΅Π½Π΅ ΠšΡƒΠ½Π°Π΅Π²ΠΎΠΉ Π·Π° ΠΎΠ³Ρ€ΠΎΠΌΠ½ΡƒΡŽ ΠΏΠΎΠΌΠΎΡ‰ΡŒ Π² Ρ€Π°Π±ΠΎΡ‚Π΅, Π·Π° ΠΎΡ‡Π΅Π½ΡŒ Π²Π½ΠΈΠΌΠ°Ρ‚Π΅Π»ΡŒΠ½ΠΎΠ΅ ΠΊΠΎ ΠΌΠ½Π΅ ΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΠ΅ ΠΈ Π·Π° ΠΏΠΎΡΡ‚ΠΎΡΠ½Π½ΡƒΡŽ Π·Π°Π±ΠΎΡ‚Ρƒ ΠΎ Π²ΡΠ΅ΠΉ Π»Π°Π±ΠΎΡ€Π°Ρ‚ΠΎΡ€ΠΈΠΈ. ОсобСнно Ρ…ΠΎΡ‡Ρƒ ΠΎΡ‚ΠΌΠ΅Ρ‚ΠΈΡ‚ΡŒ ΠΈΡ… Π½Π΅Π·Π°ΠΌΠ΅Π½ΠΈΠΌΡ‹ΠΉ Ρ‚Ρ€ΡƒΠ΄ ΠΈ ΠΏΠΎΡΡ‚ΠΎΡΠ½Π½ΡƒΡŽ Π³ΠΎΡ‚ΠΎΠ²Π½ΠΎΡΡ‚ΡŒ ΠΎΠ±Π»Π΅Π³Ρ‡ΠΈΡ‚ΡŒ Ρ€Π°Π±ΠΎΡ‚Ρƒ экспСримСнтатора. Π’Π°ΠΊΠΆΠ΅ я Π±Π»Π°Π³ΠΎΠ΄Π°Ρ€ΡŽ Π·Π° ΠΏΠΎΠΌΠΎΡ‰ΡŒ Нину Π“Ρ€ΠΈΡˆΠΈΠ½Ρƒ.

Π― ΠΎΡ‡Π΅Π½ΡŒ ΠΏΡ€ΠΈΠ·Π½Π°Ρ‚Π΅Π»Π΅Π½ ΠΌΠΎΠΈΠΌ Π±ΠΎΠ»Π΅Π΅ ΡΡ‚Π°Ρ€ΡˆΠΈΠΌ ΠΊΠΎΠ»Π»Π΅Π³Π°ΠΌ: Π•Π»Π΅Π½Π΅ Π”Π°Π²Ρ‹Π΄ΠΎΠ²ΠΎΠΉ, ΠžΠ»Π΅Π³Ρƒ ДСнисСнко, ΠŸΠ΅Ρ‚Ρ€Ρƒ Π‘ΠΈΠΌΠΎΠ½Π΅Π½ΠΊΠΎ, ΠΠ»ΡŒΠ±Π΅Ρ€Ρ‚Ρƒ Π‘ΠΈΡ‚ΠΈΠΊΠΎΠ²Ρƒ ΠΈ Π•Π»ΠΈΠ·Π°Π²Π΅Ρ‚Π΅ ΠšΠΎΠ²Ρ€ΠΈΠ³ΠΈΠ½ΠΎΠΉ, Π·Π° Π²Π½ΠΈΠΌΠ°Π½ΠΈΠ΅, ΠΊΠΎΡ‚ΠΎΡ€ΠΎΠ΅ ΠΎΠ½ΠΈ ΠΌΠ½Π΅ удСляли ΠΈ Π·Π° ΠΏΠΎΡΡ‚ΠΎΡΠ½Π½ΡƒΡŽ ΠΏΠΎΠΌΠΎΡ‰ΡŒ ΠΈ ΠΏΠΎΠ»Π΅Π·Π½Ρ‹Π΅ совСты.

Бпасибо большоС ΠœΠ°Ρ€ΠΈΠΈ ΠœΠ°Ρ‚Ρ‹Π³ΠΈΠ½ΠΎΠΉ, ΠœΠ°ΠΊΡΠΈΠΌΡƒ НСкрасову, НадСТдС Поповой, Π‘Π΅Ρ€Π³Π΅ΡŽ Π“ΡƒΡ€ΡŒΡΠ½ΠΎΠ²Ρƒ, Π”ΠΌΠΈΡ‚Ρ€ΠΈΡŽ Лябину ΠΈ ΠšΠΈΡ€ΠΈΠ»Π»Ρƒ БтасСвичу Π·Π° Π΄Ρ€ΡƒΠΆΠ΅ΡΠΊΠΎΠ΅ ΠΎΡ‚Π½ΠΎΡˆΠ΅Π½ΠΈΠ΅ ΠΈ Π³ΠΎΡ‚ΠΎΠ²Π½ΠΎΡΡ‚ΡŒ всСгда ΠΏΠΎΠΌΠΎΡ‡ΡŒ.

Π― ΠΎΡ‡Π΅Π½ΡŒ ΠΏΡ€ΠΈΠ·Π½Π°Ρ‚Π΅Π»Π΅Π½ Π•Π²Π³Π΅Π½ΠΈΠΈ Π’ΠΈΠΊΡ‚ΠΎΡ€ΠΎΠ²Π½Π΅ Π‘Π΅Ρ€Π΅Π±Ρ€ΠΎΠ²ΠΎΠΉ Π·Π° ΠΏΠΎΠΌΠΎΡ‰ΡŒ Π² Π½Π°ΠΏΠΈΡΠ°Π½ΠΈΠΈ диссСртационной Ρ€Π°Π±ΠΎΡ‚Ρ‹.

Π‘Π»Π°Π³ΠΎΠ΄Π°Ρ€ΡŽ Ρ‚Π°ΠΊΠΆΠ΅ всСх сотрудников Π˜Π½ΡΡ‚ΠΈΡ‚ΡƒΡ‚Π° Π±Π΅Π»ΠΊΠ° РАН, с ΠΊΠΎΡ‚ΠΎΡ€Ρ‹ΠΌΠΈ я Ρ€Π°Π±ΠΎΡ‚Π°Π» ΠΈ ΠΎΠ±Ρ‰Π°Π»ΡΡ.

ΠŸΠΎΠΊΠ°Π·Π°Ρ‚ΡŒ вСсь тСкст

Бписок Π»ΠΈΡ‚Π΅Ρ€Π°Ρ‚ΡƒΡ€Ρ‹

  1. Adam, S.A., Nakagawa, Π’., Swanson, M.S., Woodruff, Π’.К. and Dreyfuss, G. (1986) mRNA polyaderiylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Mol Cell Biol, 6, 2932−2943.
  2. Afonina, E., Stauber, R. and Pavlakis, G.N. (1998) The human poly (A)-binding protein 1 shuttles between the nucleus and the cytoplasm. J Biol Chem, 273, 13 015−13 021.
  3. Allain, F.H., Bouvet, P., Dieckmann, T. and Feigon, J. (2000) Molecular basis of sequence-specific recognition of pre-ribosomal RNA by nucleolin. Embo J, 19, 6870−6881.
  4. Altmann, M., Wittmer, Π’., Methot, N., Sonenberg, N. and Trachsel, H. (1995) The Saccharomyces cerevisiae translation initiation factor Tif3 and its mammalian homologue, eIF-4B, have RNA annealing activity. Embo J, 14, 3820−3827.
  5. Baer, B.W. and Kornberg, R.D. (1980) Repeating structure of cytoplasmic poly (A)-ribonucleoprotein. Proc Natl Acad Sci USA, 77, 1890−1892.
  6. Baer, B.W. and Kornberg, R.D. (1983) The protein responsible for the repeating structure of cytoplasmic poly (A)-ribonucleoprotein. J Cell Biol, 96, 717−721.
  7. Bag, J. (1984) Cytoplasmic mRNA-protein complexes of chicken muscle cells and their role in protein synthesis. Eur JBiochem, 141, 247−254.
  8. Bagga, P. S., Arhin, G.K. and Wilusz, J. (1998) DSEF-1 is a member of the hnRNP H family of RNA-binding proteins and stimulates pre-mRNA cleavage and polyadenylation in vitro. Nucleic Acids Res, 26, 5343−5350.
  9. Balda, M.S. and Matter, K. (2000) The tight junction protein ZO-1 and an interacting transcription factor regulate ErbB-2 expression. Embo J, 19, 2024−2033.
  10. Balda, M.S., Garrett, M.D. and Matter, K. (2003) The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. J Cell Biol, 160, 423−432.
  11. Baltimore, D. and Huang, A.S. (1970) Interaction of HeLa cell proteins with RNA. J Mol Biol, 47, 263−273.
  12. Barnett, S.F., Friedman, D.L. and LeStourgeon, W.M. (1989) The Π‘ proteins of HeLa 40S nuclear ribonucleoprotein particles exist as anisotropic tetramers of (Cl)3 C2. Mol Cell Biol, 9, 492−498.
  13. Barnett, S.F., Theiry, T.A. and LeStourgeon, W.M. (1991) The core proteins A2 and Bl exist as (A2)3B1 tetramers in 40S nuclear ribonucleoprotein particles. Mol Cell Biol, 11, 864−871.
  14. Belitsina, N.V., Ovchinnikov, L.P., Spirin, A.S., Gendon, Y.Z. and Chernos, V.I. (1968) The informosomes of HeLe cells infected by smallpoxvaccine virus. Mol. Biol. (USSR), 2, 727−735.
  15. Belsham, G.J. and Sonenberg, N. (2000) Picornavirus RNA translation: roles for cellular proteins. Trends Microbiol, 8, 330−335.
  16. Bennett, M., Pinol-Roma, S., Staknis, D., Dreyfuss, G. and Reed, R. (1992) Differential binding of heterogeneous nuclear ribonucleoproteins to mRNA precursors prior to spliceosome assembly in vitro. Mol Cell Biol, 12, 3165−3175.
  17. Berglund, J.A., Fleming, M.L. and Rosbash, M. (1998) The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequence. Rna, 4, 998−1006.
  18. Bernstein, P., Peltz, S.W. and Ross, J. (1989) The poly (A)-poly (A)-binding protein complex is a major determinant of mRNA stability in vitro. Mol Cell Biol, 9, 659−670.
  19. Beyer, A.L., Christensen, M.E., Walker, B.W. and LeStourgeon, W.M. (1977) Identification and characterization of the packaging proteins of core 40S hnRNP particles. Cell, 11, 127 138.
  20. Beyer, A.L. and Osheim, Y.N. (1990) In Strauss, P. and Wilson, S. (eds.), The Eukaryotic Nucleus: Structure and Function. Telford, Caldwell, Vol. 2, p. 431.
  21. Bi, X. and Goss, D.J. (2000) Wheat germ poly (A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4 °F. J Biol Chem, 275, 17 740−17 746.
  22. Biamonti, G" Buvoli, M., Bassi, M.T., Morandi, C., Cobianchi, F. and Riva, S. (1989) Isolation of an active gene encoding human hnRNP protein Al. Evidence for alternative splicing. J Mol Biol, 207, 491−503.
  23. Biamonti, G. and Riva, S. (1994) New insights into the auxiliary domains of eukaryotic RNA binding proteins. FEBS Lett, 340, 1−8.
  24. , H.C. (1983) A rapid alkaline extraction method for the isolation of plasmid DNA. Methods Enzymol, 100, 243−255.
  25. , G. (1972) Protein tightly bound to globin mRNA. Biochem Biophys Res Commun, 47,88−95.
  26. , G. (1973) A protein of molecular weight 78,000 bound to the polyadenylate region of eukaryotic messenger RNAs. Proc Natl Acad Sci USA, 70, 924−928.
  27. Boeck, R., Tarun, S., Jr., Rieger, M., Deardorff, J.A., Muller-Auer, S. and Sachs, A.B. (1996) The yeast Pan2 protein is required for poly (A)-binding protein-stimulated poly (A)-nuclease activity. J Biol Chem, 271, 432−438.
  28. Borman, A.M., Michel, Y.M., Malnou, C.E. and Kean, K.M. (2002) Free poly (A) stimulates capped mRNA translation in vitro through the eIF4G-poly (A)-binding protein interaction. J Biol Chem, 277, 36 818−36 824.
  29. Bouvet, P. and Wolffe, A.P. (1994) A role for transcription and FRGY2 in masking maternal mRNA within Xenopus oocytes. Cell, 77, 931−941.
  30. Bouvet, P., Matsumoto, K. and Wolffe, A.P. (1995) Sequence-specific RNA recognition by the Xenopus Y-box proteins. An essential role for the cold shock domain. J Biol Chem, 270, 28 297−28 303.
  31. Braddock, D.T., Baber, J.L., Levens, D. and Clore, G.M. (2002) Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP К KH3 and single-stranded DNA. EmboJ, 21, 3476−3485.
  32. Braddock, M., Muckenthaler, M., White, M.R., Thorburn, A.M., Sommerville, J., Kingsman, A.J. and Kingsman, S.M. (1994) Intron-less RNA injected into the nucleus of
  33. Xenopus oocytes accesses a regulated translation control pathway. Nucleic Acids Res, 22, 5255−5264.
  34. Braun, I.C., Rohrbach, E., Schmitt, C. and Izaurralde, E. (1999) TAP binds to the constitutive transport element (CTE) through a novel RNA-binding motif that is sufficient to promote CTE-dependent RNA export from the nucleus. Embo J, 18, 1953−1965.
  35. Braun, I.C., Herold, A., Rode, M., Conti, E. and Izaurralde, E. (2001) Overexpression of TAP/pl5 heterodimers bypasses nuclear retention and stimulates nuclear mRNA export. J Biol Chem, 276, 20 536−20 543.
  36. Braun, I.C., Herold, A., Rode, M. and Izaurralde, E. (2002) Nuclear export of mRNA by TAP/NXF1 requires two nucleoporin-binding sites but not pi5. Mol Cell Biol, 22, 54 055 418.
  37. Brostoff, S. and Eylar, E.H. (1971) Localization of methylated arginine in the Al protein from myelin. Proc Natl Acad Sci USA, 68, 765−769.
  38. Brown, C.E., Tarun, S.Z., Jr., Boeck, R. and Sachs, A.B. (1996) PAN3 encodes a subunit of the Pablp-dependent poly (A) nuclease in Saccharomyces cerevisiae. Mol Cell Biol, 16, 5744−5753.
  39. Buckanovich, R.J., Posner, J.B. and Darnell, R.B. (1993) Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding protein and is specifically expressed in the developing motor system. Neuron, 11, 657−672.
  40. Buckingham, M.E., Cohen, A. and Gros, F. (1976) Cytoplasmic distribution of pulse-labelled poly (A)-containing RNA, particularly 26 S RNA, during myoblast growth and differentiation. J Mol Biol, 103, 611−626.
  41. Burd, C.G., Matunis, E.L. and Dreyfuss, G. (1991) The multiple RNA-binding domains of the mRNA poly (A)-binding protein have different RNA-binding activities. Mol Cell Biol, 11,3419−3424.
  42. Burd, C.G. and Dreyfuss, G. (1994(A)) Conserved structures and diversity of functions of RNA-binding proteins. Science, 265, 615−621.
  43. Burd, C.G. and Dreyfuss, G. (1994(B)) RNA binding specificity of hnRNP Al: significance of hnRNP Al high- affinity binding sites in pre-mRNA splicing. Embo J, 13, 1197−1204.
  44. Burny, A., Huez, G., Marbaix, G. and Chantrenne, H. (1969) On a messenger ribonucleoprotein complex from rabbit reticulocytes. Biochim Biophys Acta, 190, 228−231.
  45. Buvoli, M., Biamonti, G., Tsoulfas, P., Bassi, M.T., Ghetti, A., Riva, S. and Morandi, C. (1988) cDNA cloning of human hnRNP protein Al reveals the existence of multiple mRNA isoforms. Nucleic Acids Res, 16, 3751−3770.
  46. Buvoli, M., Cobianchi, F., Bestagno, M.G., Mangiarotti, A., Bassi, M.T., Biamonti, G. and Riva, S. (1990) Alternative splicing in the human gene for the core protein Al generates another hnRNP protein. Embo J, 9, 1229−1235.
  47. Buvoli, M., Cobianchi, F. and Riva, S. (1992) Interaction of hnRNP Al with snRNPs and pre-mRNAs: evidence for a possible role of Al RNA annealing activity in the first steps of spliceosome assembly. Nucleic Acids Res, 20, 5017−5025.
  48. Bycroft, M., Hubbard, T.J., Proctor, M., Freund, S.M. and Murzin, A.G. (1997) The solution structure of the SI RNA binding domain: a member of an ancient nucleic acid-binding fold. Cell, 88, 235−242.
  49. Caceres, J.F. and Krainer, A.R. (1997) Mammalian pre-mRNA splicing factors. In Krainer, A.R. (ed.), Eukaryotic mRNA processing. Oxford University Press, pp. 174−212.
  50. Caponigro, G. and Parker, R. (1995) Multiple functions for the poly (A)-binding protein in mRNA decapping and deadenylation in yeast. Genes Dev, 9, 2421−2432.
  51. Capowski, E.E., Esnault, S., Bhattacharya, S. and Malter, J.S. (2001) Y box-binding factor promotes eosinophil survival by stabilizing granulocyte-macrophage colony-stimulating factor mRNA. J Immunol, 167, 5970−5976.
  52. Cartouzou, G., Attali, J.C. and Lissitzky, S. (1968) Messenger ribonucleic acids of the thyroid gland. I. Rapidly-labelled RNA of nuclei and polysomes. Eur J Biochem, 4, 41−54.
  53. Casey, J.L., Hentze, M.W., Koeller, D.M., Caughman, S.W., Rouault, T.A., Klausner, R.D. and Harford, J.B. (1988) Iron-responsive elements: regulatory RNA sequences that control mRNA levels and translation. Science, 240, 924−928.
  54. Chan, R.C. and Black, D.L. (1997) The polypyrimidine tract binding protein binds upstream of neural cell-specific c-src exon N1 to repress the splicing of the intron downstream. Mol Cell Biol, 17,4667−4676.
  55. Chang, D.D. and Sharp, P.A. (1989) Regulation by HIV Rev depends upon recognition of splice sites. Cell, 59, 789−795.
  56. , H.A., Ни, M., Hickstein, D.D. and Yang, L. (2001) Oncogenic TLS/ERG and EWS/Fli-1 fusion proteins inhibit RNA splicing mediated by YB-1 protein. Cancer Res, 61, 3586−3590.
  57. Chen, C.Y., Gherzi, R., Andersen, J.S., Gaietta, G., Jurchott, K., Royer, H.D., Mann, M. and Karin, M. (2000) Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation. Genes Dev, 14, 1236−1248.
  58. Choi, Y.D. and Dreyfuss, G. (1984) Isolation of the heterogeneous nuclear RNA-ribonucleoprotein complex (hnRNP): a unique supramolecular assembly. Proc Natl Acad Sci USA, 81,7471−7475.
  59. Choi, Y.D., Grabowski, P.J., Sharp, P.A. and Dreyfuss, G. (1986) Heterogeneous nuclear ribonucleoproteins: role in RNA splicing. Science, 231, 1534−1539.
  60. Chou, M.Y., Rooke, N. Turck, C.W. and Black, D.L. (1999) hnRNP H is a component of a splicing enhancer complex that activates a c-src alternative exon in neuronal cells. Mol Cell Biol, 19,69−77.
  61. Cobianchi, F., SenGupta, D.N., Zmudzka, B.Z. and Wilson, S.H. (1986) Structure of rodent helix-destabilizing protein revealed by cDNA cloning. J Biol Chem, 261, 3536−3543.
  62. Cobianchi, F., Biamonti, G., Maconi, M. and Riva, S. (1994) Human hnRNP protein Al: a model polypeptide for a structural and genetic investigation of a broad family of RNA binding proteins. Genetica, 94, 101−114.
  63. Cohen, I. and Reynolds, W.F. (1991) The Xenopus YB3 protein binds the Π’ box element of the class III promoter. Nucleic Acids Res, 19, 4753−4759.
  64. Conway, G., Wooley, J., Bibring, T. and LeStourgeon, W.M. (1988) Ribonucleoproteins package 700 nucleotides of pre-mRNA into a repeating array of regular particles. Mol Cell Biol, 8, 2884−2895.
  65. Cote, Π‘.A., Gautreau, D., Denegre, J.M., Kress, T.L., Terry, N.A. and Mowry, K.L. (1999) A Xenopus protein related to hnRNP I has a role in cytoplasmic RNA localization. Mol Cell, 4,431−437.
  66. Craig, A.W., Haghighat, A., Yu, A.T. and Sonenberg, N. (1998) Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature, 392, 520−523.
  67. Cristofari, G. and Darlix, J.L. (2002) The ubiquitous nature of RNA chaperone proteins. Prog Nucleic Acid Res Mol Biol, 72, 223−268.
  68. Crowder, S.M., Kanaar, R., Rio, D.C. and Alber, T. (1999) Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal. Proc Natl Acad Sci U S A, 96, 4892−4897.
  69. Crozat, A., Aman, P., Mandahl, N. and Ron, D. (1993) Fusion of CHOP to a novel RNA-binding protein in human myxoid liposarcoma. Nature, 363, 640−644.
  70. Custodio, N., Carmo-Fonseca, M., Geraghty, F., Pereira, H.S., Grosveld, F. and Antoniou, M. (1999) Inefficient processing impairs release of RNA from the site of transcription. EmboJ, 18,2855−2866.
  71. , B. (1997) A look at messenger RNP moving through the nuclear pore. Cell, 88, 585−588.
  72. , B. (2001) Assembly and transport of a premessenger RNP particle. Proc Natl Acad Sci U S A, 98, 7012−7017.
  73. Darnbrough, C.H. and Ford, P.J. (1981) Identification in Xenopus laevis of a class of oocyte-specific proteins bound to messenger RNA. Eur J Biochem, 113, 415−424.
  74. , E.H. (1986) Gene Activity in Early Development. Academic Press, New York.
  75. Davies, H.G., Giorgini, F., Fajardo, M.A. and Braun, R.E. (2000) A sequence-specific RNA binding complex expressed in murine germ cells contains MSY2 and MSY4. Dev Biol, 221, 87−100.
  76. Davydova, E.K., Evdokimova, V.M., Ovchinnikov, L.P. and Hershey, J.W. (1997) Overexpression in COS cells of p50, the major core protein associated with mRNA, results in translation inhibition. Nucleic Acids Res, 25, 2911−2916.
  77. Deardorff, J.A. and Sachs, A.B. (1997) Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly (A)-binding protein. J Mol Biol, 269, 67−81.
  78. Decker, Π‘ J. and Parker, R. (2002) mRNA decay enzymes: decappers conserved between yeast and mammals. Proc Natl Acad Sci US A, 99, 12 512−12 514.
  79. Dejgaard, K. and Leffers, H. (1996) Characterisation of the nucleic-acid-binding activity of KH domains. Different properties of different domains. Eur J Biochem, 241, 425−431.
  80. Dempsey, L.A., Hanakahi, L.A. and Maizels, N. (1998) A specific isoform of hnRNP D interacts with DNA in the LR1 heterodimer: canonical RNA binding motifs in a sequence-specific duplex DNA binding protein. J Biol Chem, 273, 29 224−29 229.
  81. Dempsey, L.A., Sun, H" Hanakahi, L.A. and Maizels, N. (1999) G4 DNA binding by LR1 and its subunits, nucleolin and hnRNP D, A role for G-G pairing in immunoglobulin switch recombination. J Biol Chem, 274, 1066−1071.
  82. Denisenko, O. and Bomsztyk, K. (2002) Yeast hnRNP K-like genes are involved in regulation of the telomeric position effect and telomere length. Mol Cell Biol, 22, 286−297.
  83. Deo, R.C., Bonanno, J.B., Sonenberg, N. and Burley, S.K. (1999) Recognition of polyadenylate RNA by the poly (A)-binding protein. Cell, 98, 835−845.
  84. Didier, D.K., Schiffenbauer, J., Woulfe, S.L., Zacheis, M. and Schwartz, B.D. (1988) Characterization of the cDNA encoding a protein binding to the major histocompatibility complex class II Y box. Proc Natl Acad Sci USA, 85, 7322−7326.
  85. Dingwall, C. and Laskey, R.A. (1991) Nuclear targeting sequences—a consensus? Trends BiochemSci, 16, 478−481.
  86. Doniger, J., Landsman, D., Gonda, M.A. and Wistow, G. (1992) The product of unr, the highly conserved gene upstream of N-ras, contains multiple repeats similar to the cold-shock domain (CSD), a putative DNA-binding motif. New Biol, 4, 389−395.
  87. Dostie, J. and Dreyfuss, G. (2002) Translation is required to remove Y14 from mRNAs in the cytoplasm. Curr Biol, 12, 1060−1067.
  88. , G. (1986) Structure and function of nuclear and cytoplasmic ribonucleoprotein particles. Annu Rev Cell Biol, 2, 459−498.
  89. Dreyfuss, G., Swanson, M.S. and Pinol-Roma, S. (1988) Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation. Trends Biochem Sci, 13, 86−91.
  90. Dreyfuss, G., Matunis, M.J., Pinol-Roma, S. and Burd, C.G. (1993) hnRNP proteins and the biogenesis of mRNA. Annu Rev Biochem, 62, 289−321.
  91. Dreyfuss, G., Kim, V.N. and Kataoka, N. (2002) Messenger-RNA-binding proteins and the messages they carry. Nat Rev Mol Cell Biol, 3, 195−205.
  92. Eckner, R, Ellmeier, W. and Birnstiel, M.L. (1991) Mature mRNA 3' end formation stimulates RNA export from the nucleus. Embo J, 10, 3513−3522.
  93. Economidis, I.V. and Pederson, T. (1983) Structure of nuclear ribonucleoprotein: heterogeneous nuclear RNA is complexed with a major sextet of proteins in vivo. Proc Natl Acad Sci USA, 80, 1599−1602.
  94. Evdokimova, V.M. and Ovchinnikov, L.P. (1999) Translational regulation by Y-box transcription factor: involvement of the major mRNA-associated protein, p50. Int J Biochem Cell Biol, 31, 139−149.
  95. Evdokimova, V., Ruzanov, P., Imataka, H., Raught, Π’., Svitkin, Y., Ovchinnikov, L.P. and Sonenberg, N. (2001) The major mRNA-associated protein YB-1 is a potent 5' cap-dependent mRNA stabilizer. Embo J, 20, 5491−5502.
  96. Eversole, A. and Maizels, N. (2000) In vitro properties of the conserved mammalian protein hnRNP D suggest a role in telomere maintenance. Mol Cell Biol, 20, 5425−5432.
  97. Fakan, S., Leser, G. and Martin, Π’.Π•. (1986) Immunoelectron microscope visualization of nuclear ribonucleoprotein antigens within spread transcription complexes. J Cell Biol, 103, 1153−1157.
  98. Foe, V.E., Wilkinson, L.E. and Laird, C.D. (1976) Comparative organization of active transcription units in Oncopeltus fasciatus. Cell, 9, 131−146.
  99. Ford, P.J., Mathieson, T. and Rosbash, M. (1977) Very long-lived messenger RNA in ovaries of Xenopus laevis. Dev Biol, 57, 417−426.
  100. Franke, W.W. and Scheer, U. (1974) Pathways of nucleocytoplasmic translocation of ribonucleoproteins. Symp Soc Exp Biol, 249−282.
  101. Fribourg, S., Braun, I.C., Izaurralde, E. and Conti, E. (2001) Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/pl5 mRNA nuclear export factor. Mol Cell, 8, 645−656.
  102. , D.R. (1991) The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev, 5, 2108−2116.
  103. , D.R. (1998) A tale of two termini: a functional interaction between the termini of an mRNA is a prerequisite for efficient translation initiation. Gene, 216, 1−11.
  104. Gatfield, D., Le Hir, H., Schmitt, C" Braun, I.C., Kocher, Π’., Wilm, M. and Izaurralde, E. (2001) The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila. Curr Biol, 11, 1716−1721.
  105. Gatfield, D. and Izaurralde, E. (2002) REFl/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J Cell Biol, 159, 579−588.
  106. Gattoni, R., Mahe, D., Mahl, P., Fischer, N., Mattei, M.G., Stevenin, J. and Fuchs, J.P. (1996) The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucleic Acids Res, 24, 2535−2542.
  107. , G.P. (1961) Ribonucleic acid of nucleolo-chromosomal apparatus. Biokhimija, 26, 1095−1107.
  108. Georgiev, G.P. and Mantieva, V.L. (1962) Isolation of DNA-like RNA and ribosomal RNA from the nucleolo-chromosomal apparatus of mammalian cells. Biochim. Biophys. Acta, 61, 153−154.
  109. Georgiev, G.P., Samarina, O.P., Lerman, M.I. and Smirnov, N.V. (1963) Biosynthesis of messenger and ribosomal RNA in nucleolo-chromosomal apparatus of animal cell. Nature, 200, 1291−1294.
  110. Ghisolfi, L., Joseph, G., Amalric, F. and Erard, M. (1992) The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties. J Biol Chem, 267, 2955−2959.
  111. Gingras, A.C., Raught, B. and Sonenberg, N. (1999) eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation. Annu Rev Biochem, 68, 913−963.
  112. Giorgini, F., Davies, H.G. and Braun, R.E. (2001) MSY2 and MSY4 bind a conserved sequence in the 3' untranslated region of protamine 1 mRNA in vitro and in vivo. Mol Cell Biol, 21, 7010−7019.
  113. Goldstein, J., Pollitt, N.S. and Inouye, M. (1990) Major cold shock protein of Escherichia coli. Proc Natl Acad Sci USA, 87, 283−287.
  114. Gonda, K., Fowler, J., Katoku-Kikyo, N., Haroldson, J., Wudel, J. and Kikyo, N. (2003) Reversible disassembly of somatic nucleoli by the germ cell proteins FRGY2a and FRGY2b. Nat Cell Biol, 5, 205−210.
  115. Gorlach, M., Wittekind, M., Beckman, R.A., Mueller, L. and Dreyfuss, G. (1992) Interaction of the RNA-binding domain of the hnRNP Π‘ proteins with RNA. Embo /, 11, 3289−3295.
  116. Gorlach, M., Burd, C.G. and Dreyfuss, G. (1994) The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein Π‘ proteins. J Biol Chem, 269, 23 074−23 078.
  117. Grange, Π’., de Sa, C.M., Oddos, J. and Pictet, R. (1987) Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif. Nucleic Acids Res, 15, 4771 -4787.
  118. Grant, C.E. and Deeley, R.G. (1993) Cloning and characterization of chicken YB-1: regulation of expression in the liver. Mol Cell Biol, 13, 4186−4196.
  119. Grant, R.P., Hurt, E., Neuhaus, D. and Stewart, M. (2002) Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXFl. Nat Struct Biol, 9, 247−251.
  120. Graumann, P.L. and Marahiel, M.A. (1998) A superfamily of proteins that contain the cold-shock domain. Trends Biochem Sci, 23, 286−290.
  121. Gray, N.K., Coller, J.M., Dickson, K.S. and Wickens, M. (2000) Multiple portions of poly (A)-binding protein stimulate translation in vivo. Embo J, 19, 4723−4733.
  122. , J.R. (1980) Proteins crosslinked to messenger RNA by irradiating polyribosomes with ultraviolet light. Nucleic Acids Res, 8, 5685−5701.
  123. , J.R. (1981) The polyribosomal mRNA—protein complex is a dynamic structure. Proc Natl Acad Sci USA, 78, 2923−2926.
  124. Gruter, P., Tabernero, C., von Kobbe, C., Schmitt, C., Saavedra, C., Bachi, A., Wilm, M., Felber, B.K. and Izaurralde, E. (1998) TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol Cell, 1, 649−659.
  125. Gu, W., Tekur, S., Reinbold, R, Eppig, J.J., Choi, Y.C., Zheng, J.Z., Murray, M.T. and Hecht, N.B. (1998) Mammalian male and female germ cells express a germ cell-specific Y-Box protein, MSY2. Biol Reprod, 59, 1266−1274.
  126. Gurdon, J.B. and Brown, D.D. (1965) Cytoplasmic Regulation of Rna Synthesis and Nucleolus Formation in Developing Embryos of Xenopus Laevis. J Mol Biol, 12, 27−35.
  127. , K.B. (2002) RNA-protein interactions. Curr Opin Struct Biol, 12, 283−288.
  128. Hamm, J. and Mattaj, I.W. (1990) Monomethylated cap structures facilitate RNA export from the nucleus. Cell, 63, 109−118.
  129. Handa, N., Nureki, O., Kurimoto, K., Kim, I., Sakamoto, H., Shimura, Y., Muto, Y. and Yokoyama, S. (1999) Structural basis for recognition of the tra mRNA precursor by the Sex- lethal protein. Nature, 398, 579−585.
  130. , G.J. (2002) RNA interference. Nature, 418, 244−251.
  131. Hayman, M.L. and Read, L.K. (1999) Trypanosoma brucei RBP16 is a mitochondrial Y-box family protein with guide RNA binding activity. J Biol Chem, 274, 12 067−12 074.
  132. , E.C. (1968) Messenger RNA in rat liver polyribosomes: evidence that it exists as ribonucleoprotein particles. J Mol Biol, 36, 401−411.
  133. Herold, A., Klymenko, T. and Izaurralde, E. (2001) NXFl/pl5 heterodimers are essential for mRNA nuclear export in Drosophila. Rna, 1, 1768−1780.
  134. Herrick, G. and Alberts, B. (1976) Nucleic acid helix-coil transitions mediated by helix-unwinding proteins from calf thymus. J Biol Chem, 251, 2133−2141.
  135. , D. (1995) RNA chaperones and the RNA folding problem. J Biol Chem, 270, 20 871−20 874.
  136. Hoek, K.S., Kidd, G.J., Carson, J.H. and Smith, R. (1998) hnRNP A2 selectively binds the cytoplasmic transport sequence of myelin basic protein mRNA. Biochemistry, 37, 7021−7029.
  137. Huang, Y. and Steitz, J.A. (2001) Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol Cell, 7, 899−905.
  138. Huang, Y., Gattoni, R., Stevenin, J. and Steitz, J.A. (2003) SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol Cell, 11, 837−843.
  139. Huez, G., Burny, A., Marbaix, G. and Lebleu, B. (1967) Release of messenger RNA from rabbit reticulocyte polyribosomes at low concentration of divalent cations. Biochim Biophys Acta, 145, 629−636.
  140. Hunt, S.L., Hsuan, J.J., Totty, N. and Jackson, R.J. (1999) unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes Dev, 13, 437−448.
  141. Iizuka, N., Najita, L., Franzusoff, A. and Samow, P. (1994) Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol Cell Biol, 14, 7322−7330.
  142. Imataka, H., Gradi, A. and Sonenberg, N. (1998) A newly identified N-terminal amino acid sequence of human eIF4G binds poly (A)-binding protein and functions in poly (A)-dependent translation. Embo J, 17, 7480−7489.
  143. Irwin, D., Kumar, A. and Malt, R.A. (1975) Messenger ribonucleoprotein complexes isolated with oligo (dT)-cellulose chromatography from kidney polysomes. Cell, 4, 157−165.
  144. Ito, K., Tsutsumi, K., Kuzumaki, Π’., Gomez, P.F., Otsu, K. and Ishikawa, K. (1994) A novel growth-inducible gene that encodes a protein with a conserved cold-shock domain. Nucleic Acids Res, 22, 2036−2041.
  145. Izaurralde, E., Jarmolowski, A., Beisel, C., Mattaj, I.W., Dreyfuss, G. and Fischer, U. (1997) A role for the M9 transport signal of hnRNP Al in mRNA nuclear export. J Cell Biol, 137, 27−35.
  146. Izaurralde, E. and Adam, S. (1998) Transport of macromolecules between the nucleus and the cytoplasm. Rna, 4, 351−364.
  147. Jacobson, A. and Peltz, S.W. (1996) Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells. Annu Rev Biochem, 65, 693−739.
  148. Jain, S.K., Pluskal, M.G. and Sarkar, S. (1979) Thermal chromatography of eukaryotic messenger ribonucleoprotein particles on oligo (dT)-cellulose. Evidence for common mRNA-associated proteins in various cell types. FEBSLett, 97, 84−90.
  149. Jensen, K.B., Musunuru, К., Lewis, H.A., Burley, S.K. and Darnell, R.B. (2000) The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain. Proc Natl Acad Sci USA, 97, 5740−5745.
  150. Jiang, W., Fang, L. and Inouye, M. (1996) The role of the 5'-end untranslated region of the mRNA for CspA, the major cold-shock protein of Escherichia coli, in cold-shock adaptation. JBacteriol, 178, 4919−4925.
  151. Jiang, W., Hou, Y. and Inouye, M. (1997) CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone. J Biol Chem, 272, 196−202.
  152. Jin, P. and Warren, S.T. (2003) New insights into fragile X syndrome: from molecules to neurobehaviors. Trends Biochem Sci, 28, 152−158.
  153. Jones, P.G., VanBogelen, R.A. and Neidhardt, F.C. (1987) Induction of proteins in response to low temperature in Escherichia coli. J Bacteriol, 169, 2092−2095.
  154. Jones, P.G. and Inouye, M. (1994) The cold-shock response—a hot topic. Mol Microbiol, 11,811−818.
  155. Kafatos, F.C. and Reich, J. (1968) Stability of differentiation-specific and nonspecific messenger RNA in insect cells. Proc Natl Acad Sci USA, 60, 1458−1465.
  156. Kaminski, A., Hunt, S.L., Patton, J.G. and Jackson, R.J. (1995) Direct evidence that polypyrimidine tract binding protein (PTB) is essential for internal initiation of translation of encephalomyocarditis virus RNA. Rna, 1, 924−938.
  157. Kandala, J.C. and Guntaka, R.V. (1994) Cloning of Rous sarcoma virus enhancer factor genes. I. Evidence that RSV-EF-I is related to Y-box (inverted CCAAT) binding proteins and binds to multiple motifs in the RSV enhancer. Virology, 198, 514−523.
  158. Karlson, D., Nakaminami, K., Toyomasu, T. and Imai, R. (2002) A cold-regulated nucleic acid-binding protein of winter wheat shares a domain with bacterial cold shock proteins. J Biol Chem, 277, 35 248−35 256.
  159. Karlson, D. and Imai, R. (2003) Conservation of the cold shock domain protein family in plants. Plant Physiol, 131, 12−15.
  160. Karpel, R.L., Miller, N.S. and Fresco, J.R. (1982) Mechanistic studies of ribonucleic acid renaturation by a helix-destabilizing protein. Biochemistry, 21, 2102−2108.
  161. Katahira, J., Strasser, K., Podtelejnikov, A., Mann, M., Jung, J.U. and Hurt, E. (1999) The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. Embo J, 18, 2593−2609.
  162. Katsu, Y., Yamashita, M. and Nagahama, Y. (1997) Isolation and characterization of goldfish Y box protein, a germ-cell-specific RNA-binding protein. Eur J Biochem, 249, 854 861.
  163. Kessler, S.H. and Sachs, A.B. (1998) RNA recognition motif 2 of yeast Pablp is required for its functional interaction with eukaryotic translation initiation factor 4G. Mol Cell Biol, 18, 51−57.
  164. Khaleghpour, K., Kahvejian, A., De Crescenzo, G., Roy, G., Svitkin, Y.V., Imataka, H., O’Connor-McCourt, M. and Sonenberg, N. (2001a) Dual interactions of the translational repressor Paip2 with poly (A) binding protein. Mol Cell Biol, 21, 5200−5213.
  165. Khaleghpour, K., Svitkin, Y.V., Craig, A.W., DeMaria, C.T., Deo, R.C., Burley, S.K. and Sonenberg, N. (2001b) Translational repression by a novel partner of human poly (A) binding protein, Paip2. Mol Cell, 7, 205−216.
  166. Kick, D., Barrett, P., Cummings, A. and Sommerville, J. (1987) Phosphorylation of a 60 kDa polypeptide from Xenopus oocytes blocks messenger RNA translation. Nucleic Acids Res, 15,4099−4109.
  167. Kiesler, E., Miralles, F. and Visa, N. (2002) HEL/UAP56 binds cotranscriptionally to the Balbiani ring pre-mRNA in an intron-independent manner and accompanies the BR mRNP to the nuclear pore. Curr Biol, 12, 859−862.
  168. Kiledjian, M. and Dreyfuss, G. (1992) Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. Embo Π£, 11, 2655−2664.
  169. Kiledjian, M., Burd, C.G., Gorlach, M., Portman, D. and Dreyfuss, G. (1994) Structure and function of hnRNP proteins. In Mattaj, I.W. and Nagai, K. (eds.), RNA-protein interactions. Oxford University press, p. 127.
  170. Kiledjian, M., Wang, X. and Liebhaber, S.A. (1995) Identification of two KH domain proteins in the alpha-globin rnRNP stability complex. Embo J, 14, 4357−4364.
  171. Kiledjian, M., DeMaria, C.T., Brewer, G. and Novick, K. (1997) Identification of AUF1 (heterogeneous nuclear ribonucleoprotein D) as a component of the alpha-globin mRNA stability complex. Mol Cell Biol, 17, 4870−4876.
  172. Kim, M.K. and Nikodem, V.M. (1999) hnRNP U inhibits carboxy-terminal domain phosphorylation by TFIIH and represses RNA polymerase II elongation. Mol Cell Biol, 19, 6833−6844.
  173. Kim, S., Park, G.H. and Paik, W.K. (1998) Recent advances in protein methylation: enzymatic methylation of nucleic acid binding proteins. Amino Acids, 15, 291−306.
  174. Kloks, C.P., Spronk, C.A., Lasonder, E., Hoffmann, A., Vuister, G.W., Grzesiek, S. and Hilbers, C.W. (2002) The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1. J Mol Biol, 316, 317−326.
  175. Kohno, K., Izumi, H., Uchiumi, Π’., Ashizuka, M. and Kuwano, M. (2003) The pleiotropic functions of the Y-box-binding protein, YB-1. Bioessays, 25, 691−698.
  176. Koike, K, Uchiumi, Π’., Ohga, Π’., Toh, S., Wada, M., Kohno, K. and Kuwano, M. (1997) Nuclear translocation of the Y-box binding protein by ultraviolet irradiation. FEBS Lett, All, 390−394.
  177. Kolluri, R. and Kinniburgh, A J. (1991) Full length cDNA sequence encoding a nuclease-sensitive element DNA binding protein. Nucleic Acids Res, 19, 4771.
  178. Kolluri, R., Torrey, T.A. and Kinniburgh, A.J. (1992) A CT promoter element binding protein: definition of a double-strand and a novel single-strand DNA binding motif. Nucleic Acids Res, 20, 111−116.
  179. Koloteva-Levine, N., Amichay, M. and Elroy-Stein, O. (2002) Interaction of hnRNP-C1/C2 proteins with RNA: analysis using the yeast three-hybrid system. FEBS Lett, 523, 7378.
  180. Korner, C.G., Wormington, M., Muckenthaler, M., Schneider, S., Dehlin, E. and Wahle, E. (1998) The deadenylating nuclease (DAN) is involved in poly (A) tail removal during the meiotic maturation of Xenopus oocytes. Embo J, 17, 5427−5437.
  181. Kozlov, G., Trempe, J.F., Khaleghpour, K., Kahvejian, A., Ekiel, I. and Gehring, K. (2001) Structure and function of the C-terminal PABC domain of human poly (A)-binding protein. Proc Natl Acad Sci US A, 98, 4409−4413.
  182. Kranz, J.K. and Hall, K.B. (1998) RNA binding mediates the local cooperativity between the beta-sheet and the C-terminal tail of the human U1A RJBD1 protein. J Mol Biol, 275,465−481.
  183. Kranz, J.K. and Hall, K.B. (1999) RNA recognition by the human U1A protein is mediated by a network of local cooperative interactions that create the optimal binding surface. J Mol Biol, 285,215−231.
  184. Krecic, A.M. and Swanson, M.S. (1999) hnRNP complexes: composition, structure, and function. Curr Opin Cell Biol, 11, 363−371.
  185. Kudo, S., Mattei, M.G. and Fukuda, M. (1995) Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domain. Eur J Biochem, 231, 72−82.
  186. Kuhn, U. and Pieler, T. (1996) Xenopus poly (A) binding protein: functional domains in RNA binding and protein-protein interaction. J Mol Biol, 256, 20−30.
  187. Kumar, A. and Pederson, T. (1975) Comparison of proteins bound to heterogeneous nuclear RNA and messenger RNA in HeLa cells. J Mol Biol, 96, 353−365.
  188. Kumar, A., Williams, K.R. and Szer, W. (1986) Purification and domain structure of core hnRNP proteins Al and A2 and their relationship to single-stranded DNA-binding proteins. J Biol Chem, 261, 11 266−11 273.
  189. Kumar, A. and Wilson, S.H. (1990) Studies of the strand-annealing activity of mammalian hnRNP complex protein Al. Biochemistry, 29, 10 717−10 722.
  190. Kwan, S.W. and Brawerman, G. (1972) A particle associated with the polyadenylate segment in mammalian messenger RNA. Proc Natl Acad Sci U S A, 69, 3247−3250.
  191. Kwon, S., Barbarese, E. and Carson, J.H. (1999) The cis-acting RNA trafficking signal from myelin basic protein mRNA and its cognate trans-acting ligand hnRNP A2 enhance cap-dependent translation. J Cell Biol, 147, 247−256.
  192. Kwon, Y.K., Murray, M.T. and Hecht, N.B. (1993) Proteins homologous to the Xenopus germ cell-specific RNA-binding proteins p54/p56 are temporally expressed in mouse male germ cells. Dev Biol, 158, 99−100.
  193. LaBranche, H., Dupuis, S., Ben-David, Y., Bani, M.R., Wellinger, R.J. and Chabot, B. (1998) Telomere elongation by hnRNP Al and a derivative that interacts with telomeric repeats and telomerase. Nat Genet, 19, 199−202.
  194. Ladomery, M. and Sommerville, J. (1994) Binding of Y-box proteins to RNA: involvement of different protein domains. Nucleic Acids Res, 22, 5582−5589.
  195. , U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680−685.
  196. , D. (1992) RNP-1, an RNA-binding motif is conserved in the DNA-binding cold shock domain. Nucleic Acids Res, 20, 2861−2864.
  197. Le Hir, H., Nott, A. and Moore, M.J. (2003) How introns influence and enhance eukaryotic gene expression. Trends Biochem Sci, 28, 215−220.
  198. Lee, C.G., Zamore, P.D., Green, M.R. and Hurwitz, J. (1993) RNA annealing activity is intrinsically associated with U2AF. J Biol Chem, 268, 13 472−13 478.
  199. Legrain, P. and Rosbash, M. (1989) Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell, 57, 573−583.
  200. Lewis, H.A., Chen, H., Edo, C., Buckanovich, R.J., Yang, Y.Y., Musunuru, K., Zhong, R., Darnell, R.B. and Burley, S.K. (1999) Crystal structures of Nova-1 and Nova-2 K-homology RNA-binding domains. Structure FoldDes, 7, 191−203.
  201. Lewis, H.A., Musunuru, K., Jensen, K.B., Edo, C., Chen, H., Darnell, R.B. and Burley, S.K. (2000) Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome. Cell, 100, 323−332.
  202. Libri, D., Graziani, N., Saguez, C. and Boulay, J. (2001) Multiple roles for the yeast SUB2/yUAP56 gene in splicing. Genes Dev, 15, 36−41.
  203. Liker, E., Fernandez, E., Izaurralde, E. and Conti, E. (2000) The structure of the mRNA export factor TAP reveals a cis arrangement of a non-canonical RNP domain and an LRR domain. Embo J, 19, 5587−5598.
  204. Lindberg, U. and Sundquist, B. (1974) Isolation of messenger ribonucleoproteins from mammalian cells. J Mol Biol, 86,451−468.
  205. Liu, Q. and Dreyfuss, G. (1995) In vivo and in vitro arginine methylation of RNA-binding proteins. Mol Cell Biol, 15, 2800−2808.
  206. Lloberas, J., Maki, RA. and Celada, A. (1995) Repression of major histocompatibility complex I-A beta gene expression by dbpA and dbpB (mYB-1) proteins. Mol Cell Biol, 15, 5092−5099.
  207. Lothstein, L., Arenstorf, H.P., Chung, S.Y., Walker, B.W., Wooley, J.C. and LeStourgeon, W.M. (1985) General organization of protein in HeLa 40S nuclear ribonucleoprotein particles. J Cell Biol, 100, 1570−1581.
  208. Lou, H., Helfman, D.M., Gagel, R.F. and Berget, S.M. (1999) Polypyrimidine tract-binding protein positively regulates inclusion of an alternative 3'-terminal exon. Mol Cell Biol, 19, 78−85.
  209. Lu, S. and Cullen, B.R. (2003) Analysis of the stimulatory effect of splicing on mRNA production and utilization in mammalian cells. Rna, 9, 618−630.
  210. Lukanidin, E.M., Zalmanzon, E.S., Komaromi, L., Samarina, O.P. and Georgiev, G.P. (1972) Structure and function of informofers. Nat New Biol, 238, 193−197.
  211. Luo, M.L., Zhou, Z., Magni, K., Christoforides, C., Rappsilber, J., Mann, M. and Reed, R. (2001) Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. Nature, 413, 644−647.
  212. Lykke-Andersen, J., Shu, M.D. and Steitz, J.A. (2000) Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell, 103,1121−1131.
  213. Lykke-Andersen, J., Shu, M.D. and Steitz, J.A. (2001) Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science, 293, 1836−1839.
  214. MacDonald, G.H., Itoh-Lindstrom, Y. and Ting, J.P. (1995) The transcriptional regulatory protein, YB-1, promotes single-stranded regions in the DRA promoter. J Biol Chem, 270, 3527−3533.
  215. Makino, Y., Ohga, Π’., Toh, S., Koike, K., Okumura, K., Wada, M., Kuwano, M. and Kohno, K. (1996) Structural and functional analysis of the human Y-box binding protein (YB-1) gene promoter. Nucleic Acids Res, 24, 1873−1878.
  216. Malcolm, D.B. and Sommerville, J. (1974) The structure of chromosome-derived ribonucleoprotein in oocytes of Triturus cristatus carnifex (Laurenti). Chromosoma, 48, 137 158.
  217. Malcolm, D.B. and Sommerville, J. (1977) The structure of nuclear ribonucleoprotein of amphibian oocytes. J Cell Sci, 24, 143−165.
  218. Manival, X., Ghisolfi-Nieto, L., Joseph, G., Bouvet, P. and Erard, M. (2001) RNA-binding strategies common to cold-shock domain- and RNA recognition motif-containing proteins. Nucleic Acids Res, 29, 2223−2233.
  219. Mansfield, J.H., Wilhelm, J.E. and Hazelrigg, T. (2002) Ypsilon Schachtel, a Drosophila Y-box protein, acts antagonistically to Orb in the oskar mRNA localization and translation pathway. Development, 129, 197−209.
  220. Marello, K., LaRovere, J. and Sommerville, J. (1992) Binding of Xenopus oocyte masking proteins to mRNA sequences. Nucleic Acids Res, 20, 5593−5600.
  221. Martin, Π’., Billings, P., Pullman, J., Stevens, B. and Kinniburgh, A. (1978) Substructure of nuclear ribonucleoprotein complexes. Cold Spring Harb Symp Quant Biol, 42, 899−909.
  222. Matsumoto, K., Wassarman, K.M. and Wolffe, A.P. (1998(A)) Nuclear history of a pre-mRNA determines the translational activity of cytoplasmic mRNA. Embo J, 17, 21 072 121.
  223. Matsumoto, K. and Wolffe, A.P. (1998(B)) Gene regulation by Y-box proteins: coupling control of transcription and translation. Trends Cell Biol, 8, 318−323.
  224. Matsumoto, К., Tanaka, K.J., Aoki, К., Sameshima, M. and Tsujimoto, M. (2003) Visualization of the reconstituted FRGY2-mRNA complexes by electron microscopy. Biochem Biophys Res Commun, 306, 53−58.
  225. Matunis, E.L., Matunis, M.J. and Dreyfuss, G. (1992(B)) Characterization of the major hnRNP proteins from Drosophila melanogaster. J Cell Biol, 116, 257−269.
  226. Matunis, M.J., Michael, W.M. and Dreyfuss, G. (1992(A)) Characterization and primary structure of the poly (C)-binding heterogeneous nuclear ribonucleoprotein complex К protein. Mol Cell Biol, 12, 164−171.
  227. Mayeda, A. and Krainer, A.R. (1992) Regulation of alternative pre-mRNA splicing by hnRNP Al and splicing factor SF2. Cell, 68, 365−375.
  228. Mayeda, A., Munroe, S.H., Caceres, J.F. and Krainer, A.R. (1994) Function of conserved domains of hnRNP Al and other hnRNP A/B proteins. Embo J, 13, 5483−5495.
  229. Mayeda, A., Munroe, S.H., Xu, R.M. and Krainer, A.R. (1998) Distinct functions of the closely related tandem RNA-recognition motifs of hnRNP Al. Rna, 4, 1111−1123.
  230. Mayrand, S. and Pederson, T. (1981) Nuclear ribonucleoprotein particles probed in living cells. Proc Natl Acad Sci USA, 78, 2208−2212.
  231. Mayrand, S., Setyono, Π’., Greenberg, J.R. and Pederson, T. (1981) Structure of nuclear ribonucleoprotein: identification of proteins in contact with poly (A)+ heterogeneous nuclear RNA in living HeLa cells .J Cell Biol, 90, 380−384.
  232. McAfee, J.G., Shahied-Milam, L., Soltaninassab, S.R. and LeStourgeon, W.M. (1996(A)) A major determinant of hnRNP Π‘ protein binding to RNA is a novel bZIP- like RNA binding domain. Rna, 2, 1139−1152.
  233. McAfee, J.G., Huang, M., Soltaninassab, S.R., Rech, J.E., Iyengar, S. and LeStourgeon, W.M. (1997) The packaging of pre-mRNA. In Krainer, A.R. (ed.), Eukaryotic mRNA Processing. Oxford University Press, pp. 68−102.
  234. Mehlin, H., Daneholt, B. and Skoglund, U. (1992) Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography. Cell, 69, 605−613.
  235. Meric, F., Matsumoto, K. and Wolffe, A.P. (1997) Regulated unmasking of in vivo synthesized maternal mRNA at oocyte maturation. A role for the chaperone nucleoplasmin. J Biol Chem, 212, 12 840−12 846.
  236. Merrill, B.M., Barnett, S.F., LeStourgeon, W.M. and Williams, K.R. (1989) Primary structure differences between proteins Π‘1 and C2 of HeLa 40S nuclear ribonucleoprotein particles. Nucleic Acids Res, 17, 8441−8449.
  237. Methot, N., Pause, A., Hershey, J.W. and Sonenberg, N. (1994) The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence. Mol Cell Biol, 14, 2307−2316.
  238. Methot, N., Song, M.S. and Sonenberg, N. (1996) A region rich in aspartic acid, arginine, tyrosine, and glycine (DRYG) mediates eukaryotic initiation factor 4B (eIF4B) self-association and interaction with eIF3. Mol Cell Biol, 16, 5328−5334.
  239. Michael, W.M., Choi, M. and Dreyfuss, G. (1995) A nuclear export signal in hnRNP Al: a signal-mediated, temperature- dependent nuclear protein export pathway. Cell, 83, 415−422.
  240. Michael, W.M., Eder, P. S. and Dreyfuss, G. (1997) The К nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP К protein. Embo J, 16, 3587−3598.
  241. Michelotti, E.F., Michelotti, G.A., Aronsohn, A.I. and Levens, D. (1996) Heterogeneous nuclear ribonucleoprotein К is a transcription factor. Mol Cell Biol, 16, 2350−2360.
  242. Mili, S., Shu, H.J., Zhao, Y. and Pinol-Roma, S. (2001) Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA. Mol Cell Biol, 21, 7307−7319.
  243. Miller, O.L., Jr. and Bakken, A.H. (1972) Morphological studies of transcription. Acta Endocrinol Suppl, 168, 155−177.
  244. Min, H., Chan, R.C. and Black, D.L. (1995) The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event. Genes Dev, 9, 2659−2671.
  245. Minich, W.B. and Ovchinnikov, L.P. (1992) Role of cytoplasmic mRNP proteins in translation. Biochimie, 74, 477−483.
  246. Minich, W.B., Maidebura, I.P. and Ovchinnikov, L.P. (1993) Purification and characterization of the major 50-kDa repressor protein from cytoplasmic mRNP of rabbit reticulocytes. Eur JBiochem, 212, 633−638.
  247. Miralles, F., Ofverstedt, L.G., Sabri, N., Aissouni, Y., Hellman, U., Skoglund, U. and Visa, N. (2000) Electron tomography reveals posttranscriptional binding of pre-mRNPs to specific fibers in the nucleoplasm. J Cell Biol, 148, 271−282.
  248. Moreira, A., Takagaki, Y., Brackenridge, S., Wollerton, M., Manley, J.L. and Proudfoot, N.J. (1998) The upstream sequence element of the C2 complement poly (A) signal activates mRNA 3' end formation by two distinct mechanisms. Genes Dev, 12, 25 222 534.
  249. Morel, C., Kayibanda, B. and Scherrer, K. (1971) Proteins associated with globin messenger RNA in avian erythroblasts: Isolation and comparison with the proteins bound to nuclear messenger-likie RNA. FEBSLett, 18, 84−88.
  250. Mourelatos, Z" Abel, L., Yong, J., Kataoka, N. and Dreyfuss, G. (2001) SMN interacts with a novel family of hnRNP and spliceosomal proteins. EmboJ, 20, 5443−5452.
  251. Muhlrad, D., Decker, C.J. and Parker, R. (1994) Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5'—>3' digestion of the transcript. Genes Dev, 8, 855−866.
  252. Munro, T.P., Magee, R.J., Kidd, G.J., Carson, J.H., Barbarese, E., Smith, L.M. and Smith, R. (1999) Mutational analysis of a heterogeneous nuclear ribonucleoprotein A2 response element for RNA trafficking. J Biol Chem, 274, 34 389−34 395.
  253. Munroe, S.H. and Dong, X.F. (1992) Heterogeneous nuclear ribonucleoprotein Al catalyzes RNA. RNA annealing. Proc Natl Acad Sci USA, 89, 895−899.
  254. Murray, M.T., Krohne, G. and Franke, W.W. (1991) Different forms of soluble cytoplasmic mRNA binding proteins and particles in Xenopus laevis oocytes and embryos. J Cell Biol, 112, 1−11.
  255. Murray, M.T., Schiller, D.L. and Franke, W.W. (1992) Sequence analysis of cytoplasmic mRNA-binding proteins of Xenopus oocytes identifies a family of RNA-binding proteins. Proc Natl Acad Sci US A, 89, 11−15.
  256. , M.T. (1994) Nucleic acid-binding properties of the Xenopus oocyte Y box protein mRNP3+4. Biochemistry, 33, 13 910−13 917.
  257. , A.G. (1993) OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences. EmboJ, 12, 861−867.
  258. Musco, G., Stier, G., Joseph, C., Castiglione Morelli, M.A., Nilges, M., Gibson, T.J. and Pastore, A. (1996) Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell, 85, 237−245.
  259. Musco, G., Kharrat, A., Stier, G., Fraternali, F., Gibson, T.J., Nilges, M. and Pastore, A. (1997) The solution structure of the first KH domain of FMR1, the protein responsible for the fragile X syndrome. Nat Struct Biol, 4, 712−716.
  260. Nagai, K., Oubridge, C., lessen, Π’.Н., Li, J. and Evans, P.R. (1990) Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature, 348, 515 520.
  261. Nakielny, S. and Dreyfuss, G. (1996) The hnRNP Π‘ proteins contain a nuclear retention sequence that can override nuclear export signals. J Cell Biol, 134, 1365−1373.
  262. Nakielny, S. and Dreyfuss, G. (1999) Transport of proteins and RNAs in and out of the nucleus. Cell, 99, 677−690.
  263. Niederberger, N., Trachsel, H. and Altmann, M. (1998) The RNA recognition motif of yeast translation initiation factor Tif3/eIF4B is required but not sufficient for RNA strand-exchange and translational activity. Rna, 4, 1259−1267.
  264. Nott, A., Meislin, S.H. and Moore, M.J. (2003) A quantitative analysis of intron effects on mammalian gene expression. Rna, 9, 607−617.
  265. Oberosler, P., Hloch, P., Ramsperger, U. and Stahl, H. (1993) p53-catalyzed annealing of complementary single-stranded nucleic acids. Embo J, 12, 2389−2396.
  266. Okamoto, Π’., Izumi, H., Imamura, Π’., Takano, H., Ise, Π’., Uchiumi, Π’., Kuwano, M. and Kohno, K. (2000) Direct interaction of p53 with the Y-box binding protein, YB-1: a mechanism for regulation of human gene expression. Oncogene, 19, 6194−6202.
  267. Ostareck, D.H., Ostareck-Lederer, A., Wilm, M., Thiele, B.J., Mann, M. and Hentze, M.W. (1997) mRNA silencing in erythroid differentiation: hnRNP К and hnRNP El regulate 15-lipoxygenase translation from the 3' end. Cell, 89, 597−606.
  268. Ostareck, D.H., Ostareck-Lederer, A., Shatsky, I.N. and Hentze, M.W. (2001) Lipoxygenase mRNA silencing in erythroid differentiation: The 3'UTR regulatory complex controls 60S ribosomal subunit joining. Cell, 104, 281−290.
  269. Otero, L.J., Ashe, M.P. and Sachs, A.B. (1999) The yeast poly (A)-binding protein Pablp stimulates in vitro poly (A)-dependent and cap-dependent translation by distinct mechanisms. Embo J, 18, 3153−3163.
  270. Oubridge, C., Ito, N., Evans, P. R, Teo, C.H. and Nagai, K. (1994) Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature, 372, 432−438.
  271. Ovchinnikov, L.P., Voronina, A.S., Stepanov, A.S., Belitsina, N.V. and Spirin, A.S. (1968) Informosome-like complexes were formed by RNA adding to animal cell homogenates. Mol. Biol. (USSR), 2, 752−763.
  272. Ozer, J., Faber, M., Chalkley, R. and Sealy, L. (1990) Isolation and characterization of a cDNA clone for the CCAAT transcription factor EFIA reveals a novel structural motif. J Biol Chem, 265, 22 143−22 152.
  273. , T. (1974) Proteins associated with heterogeneous nuclear RNA in eukaryotic cells. J Mol Biol, 83, 163−183.
  274. , T. (2000) Half a century of «the nuclear matrix». Mol Biol Cell, 11, 799 805.
  275. Pelletier, M. and Read, L.K. (2003) RBP16 is a multifunctional gene regulatory protein involved in editing and stabilization of specific mitochondrial mRNAs in Trypanosoma brucei. Rna, 9, 457−468.
  276. Perez-Canadillas, J.M. and Varani, G. (2001) Recent advances in RNA-protein recognition. Curr Opin Struct Biol, 11, 53−58.
  277. Perry, R.P. and Kelley, D.E. (1968) Messenger RNA-protein complexes and newly synthesized ribosomal subunits: analysis of free particles and components of polyribosomes. J Mol Biol, 35,37−59.
  278. Pilipenko, E.V., Pestova, T.V., Kolupaeva, V.G., Khitrina, E.V., Poperechnaya, A.N., Agol, V.I. and Hellen, C.U. (2000) A cell cycle-dependent protein serves as a template-specific translation initiation factor. Genes Dev, 14, 2028−2045.
  279. Pinol-Roma, S., Choi, Y.D., Matunis, M.J. and Dreyfuss, G. (1988) Immunopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins. Genes Dev, 2, 215−227.
  280. Pinol-Roma, S., Swanson, M.S., Gall, J.G. and Dreyfuss, G. (1989) A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts. J Cell Biol, 109, 2575−2587.
  281. Pinol-Roma, S. and Dreyfuss, G. (1992) Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature, 355, 730−732.
  282. Pokrovskaya, I.D. and Gurevich, V.V. (1994) In vitro transcription: preparative RNA yields in analytical scale reactions. Anal Biochem, 220, 420−423.
  283. , B.W. (1993) Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. Trends Biochem Sci, 18, 181−186.
  284. Portman, D.S. and Dreyfuss, G. (1994) RNA annealing activities in HeLa nuclei. Embo J, 13,213−221.
  285. Preobrazhensky, A.A. and Spirin, A.S. (1978) Informosomes and their protein components: the present state of knowledge. In Progress in Nucleic Acid Research and Molecular Biology. Acad Press Inc New York, San Francisco, London, Vol. 21, pp. 1−38.
  286. Rajagopalan, L.E., Westmark, C.J., Jarzembowski, J.A. and Malter, J.S. (1998) hnRNP Π‘ increases amyloid precursor protein (APP) production by stabilizing APP mRNA. Nucleic Acids Res, 26, 3418−3423.
  287. Rajpurohit, R" Paik, W.K. and Kim, S. (1994) Effect of enzymic methylation of heterogeneous ribonucleoprotein particle Al on its nucleic-acid binding and controlled proteolysis. Biochem J, 304, 903−909.
  288. Ramirez, C.V., Vilela, C., Berthelot, K. and McCarthy, J.E. (2002) Modulation of eukaryotic mRNA stability via the cap-binding translation complex eIF4 °F. J Mol Biol, 318, 951−962.
  289. Ranjan, M., Taftiri, S.R. and Wolffe, A.P. (1993) Masking mRNA from translation in somatic cells. Genes Dev, 7, 1725−1736.
  290. Rapp, T.B., Yang, L., Conrad, E.U., 3rd, Mandahl, N. and Chansky, H.A. (2002) RNA splicing mediated by YB-1 is inhibited by TLS/CHOP in human myxoid liposarcoma cells. J Orthop Res, 20, 723−729.
  291. Reed, R. and Hurt, E. (2002) A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell, 108, 523−531.
  292. Richter, J.D. and Smith, L.D. (1984) Reversible inhibition of translation by Xenopus oocyte-specific proteins. Nature, 309, 378−380.
  293. Rodrigues, J.P., Rode, M., Gatfield, D., Blencowe, B.J., Carmo-Fonseca, M. and Izaurralde, E. (2001) REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus. Proc Natl Acad Sci USA, 98, 1030−1035.
  294. Romig, H., Fackelmayer, F.O., Renz, A., Ramsperger, U. and Richter, A. (1992) Characterization of SAF-A, a novel nuclear DNA binding protein from HeLa cells with high affinity for nuclear matrix/scaffold attachment DNA elements. Embo J, 11, 3431−3440.
  295. Rouault, T.A., Hentze, M.W., Caughman, S.W., Harford, J.B. and Klausner, R.D. (1988) Binding of a cytosolic protein to the iron-responsive element of human ferritin messenger RNA. Science, 241, 1207−1210.
  296. Roy, G., De Crescenzo, G., Khaleghpour, K., Kahvejian, A., O’Connor-McCourt, M. and Sonenberg, N. (2002) Paipl interacts with poly (A) binding protein through two independent binding motifs. Mol Cell Biol, 22, 3769−3782.
  297. Ruzanov, P.V., Evdokimova, V.M., Korneeva, N.L., Hershey, J.W. and Ovchinnikov, L.P. (1999) Interaction of the universal mRNA-binding protein, p50, with actin: a possible link between mRNA and microfilaments. J Cell Sci, 112 (Pt 20), 34 873 496.
  298. Sachs, A.B., Bond, M.W. and Kornberg, R.D. (1986) A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression. Cell, 45, 827−835.
  299. Sachs, A.B., Davis, R.W. and Kornberg, R.D. (1987) A single domain of yeast poly (A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol Cell Biol, 7, 3268−3276.
  300. Sachs, A.B. and Davis, R.W. (1990) Translation initiation and ribosomal biogenesis: involvement of a putative rRNA helicase and RPL46. Science, 247, 1077−1079.
  301. Sachs, A.B., Sarnow, P. and Hentze, M.W. (1997) Starting at the beginning, middle, and end: translation initiation in eukaryotes. Cell, 89, 831−838.
  302. Safak, M., Gallia, G.L. and Khalili, K. (1999(A)) Reciprocal interaction between two cellular proteins, Puralpha and YB-1, modulates transcriptional activity of JCVCY in glial cells. Mol Cell Biol, 19, 2712−2723.
  303. Safak, M., Gallia, G.L., Ansari, S.A. and Khalili, K. (1999(B)) Physical and functional interaction between the Y-box binding protein YB-1 and human polyomavirus JC virus large T antigen. J Virol, 73, 10 146−10 157.
  304. Sakura, H., Maekawa, Π’., Imamoto, F., Yasuda, K. and Ishii, S. (1988) Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology. Gene, 73, 499−507.
  305. Salvetti, A., Batistoni, R., Deri, P., Rossi, L. and Sommerville, J. (1998) Expression of DjYl, a protein containing a cold shock domain and RG repeat motifs, is targeted to sites of regeneration in planarians. Dev Biol, 201, 217−229.
  306. , O.P. (1964) Distribution and properties of cytoplasmic D-RNA. Biochim. Biophys. Acta, 91, 688−691.
  307. Samarina, O.P., Asriian, I.S. and Georgiev, G.P. (1965) Isolation of nuclear nucleoproteins containing informational ribonucleic acid. Dokl Akad Nauk SSSR, 163, 1510−1513.
  308. Samarina, O.P., Krichevskaya, A.A. and Georgiev, G.P. (1966) Nuclear ribonucleoprotein particles containing messenger ribonucleic acid. Nature, 210, 1319−1322.
  309. Samarina, O.P., Molnar, J., Lukanidin, E.M., Bruskov, V.I., Krichevskaya, A.A. and Georgiev, G.P. (1967) Reversible dissociation of nuclear ribonucleoprotein particle containing mRNA into RNA and protein. J Mol Biol, 27, 187−191.
  310. Samarina, O.P., Lukanidin, E.M., Molnar, J. and Georgiev, G.P. (1968) Structural organization of nuclear complexes «containing DNA-like RNA. J Mol Biol, 33, 251−263.
  311. , O.P. (1996) hnRNP particles. BioEssays, 18, 595.
  312. Santos-Rosa, H., Moreno, H., Simos, G., Segref, A., Fahrenkrog, Π’., Pante, N. and Hurt, E. (1998) Nuclear mRNA export requires complex formation between Mex67p and Mtr2p at the nuclear pores. Mol Cell Biol, 18, 6826−6838.
  313. Sapp, M., Knippers, R. and Richter, A. (1986) DNA binding properties of a 110 kDa nucleolar protein. Nucleic Acids Res, 14, 6803−6820.
  314. Schindelin, H., Marahiel, M.A. and Heinemann, U. (1993) Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature, 364, 164−168.
  315. Schindelin, H., Jiang, W., Inouye, M. and Heinemann, U. (1994) Crystal structure of CspA, the major cold shock protein of Escherichia coli. Proc Natl Acad Sci USA, 91, 51 195 123.
  316. Schnuchel, A., Wiltscheck, R., Czisch, M., Herrler, M., Willimsky, G., Graumann, P., Marahiel, M.A. and Holak, T.A. (1993) Structure in solution of the major cold-shock protein from Bacillus subtilis. Nature, 364, 169−171.
  317. Segref, A., Sharma, K., Doye, V., Hellwig, A., Huber, J., Luhrmann, R. and Hurt, E. (1997) Mex67p, a novel factor for nuclear mRNA export, binds to both poly (A)+ RNA and nuclear pores. Embo J, 16, 3256−3271.
  318. Shahied, L., Braswell, E.H., LeStourgeon, W.M. and Krezel, A.M. (2001) An antiparallel four-helix bundle orients the high-affinity RNA binding sites in hnRNP Π‘: a mechanism for RNA chaperonin activity. J Mol Biol, 305, 817−828.
  319. Shannon, M.F., Coles, L.S., Attema, J. and Diamond, P. (2001) The role of architectural transcription factors in cytokine gene transcription. JLeukoc Biol, 69, 21−32.
  320. Shih, S.C. and Claffey, K.P. (1999) Regulation of human vascular endothelial growth factor mRNA stability in hypoxia by heterogeneous nuclear ribonucleoprotein L. J Biol Chem, 274, 1359−1365.
  321. Shnyreva, M., Schullery, D.S., Suzuki, H., Higaki, Y. and Bomsztyk, K. (2000) Interaction of two multifunctional proteins. Heterogeneous nuclear ribonucleoprotein К and Y-box-binding protein. J Biol Chem, 275, 15 498−15 503.
  322. Shyu, A.B. and Wilkinson, M.F. (2000) The double lives of shuttling mRNA binding proteins. Cell, 102, 135−138.
  323. Siomi, H., Matunis, M.J., Michael, W.M. and Dreyfuss, G. (1993) The pre-mRNA binding К protein contains a novel evolutionarily conserved motif. Nucleic Acids Res, 21, 1193−1198.
  324. Siomi, H., Choi, M., Siomi, M.C., Nussbaum, R.L. and Dreyfuss, G. (1994) Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome. Cell, 77, 33−39.
  325. Siomi, H. and Dreyfuss, G. (1995) A nuclear localization domain in the hnRNP Al protein .J Cell Biol, 129, 551−560.
  326. Siomi, H. and Dreyfuss, G. (1997) RNA-binding proteins as regulators of gene expression. Curr Opin Genet Dev, 7, 345−353.
  327. Skabkin, M.A., Evdokimova, V., Thomas, A.A. and Ovchinnikov, L.P. (2001) The major messenger ribonucleoprotein particle protein p50 (YB-1) promotes nucleic acid strand annealing. J Biol Chem, 276, 44 841−44 847.
  328. Skabkina, O.V., Skabkin, M.A., Popova, N.V., Lyabin, D.N., Penalva, L.O. and Ovchinnikov, L.P. (2003) Poly (A)-binding protein positively affects YB-1 mRNA translation through specific interaction with YB-1 mRNA. J Biol Chem, 278, 18 191−18 198.
  329. Skoglund, U., Andersson, K., Bjorkroth, Π’., Lamb, M.M. and Daneholt, B. (1983) Visualization of the formation and transport of a specific hnRNP particle. Cell, 34, 847−855.
  330. , J. (1990) RNA-binding phosphoproteins and the regulation of maternal mRNA in Xenopus. JReprodFertil Suppl, 42, 225−233.
  331. Sommerville, J., Baird, J. and Turner, B.M. (1993) Histone H4 acetylation and transcription in amphibian chromatin. J Cell Biol, 120, 277−290.
  332. Sommerville, J. and Ladomery, M. (1996) Masking of mRNA by Y-box proteins. FasebJ, 10,435−443.
  333. , J. (1999) Activities of cold-shock domain proteins in translation control. Bioessays, 21, 319−325.
  334. Sonenberg, N. and Dever, Π’.Π•. (2003) Eukaryotic translation initiation factors and regulators. Curr Opin Struct Biol, 13, 56−63.
  335. , A.S. (1964) Informational RNA in early embryogenesis. J Gen Biol (USSR), 24,321−338.
  336. Spirin, A.S., Belitsina, N.V. and Lerman, M.I. (1965) Use of formaldehyde fixation for studies of ribonucleoprotein particles by caesium chloride density-gradient centrifugation. J Mol Biol, 14, 611−615.
  337. , A.S. (1969) The second Sir Hans Krebs Lecture. Informosomes. Eur J Biochem, 10, 20−35.
  338. , A.S. (1979) Messenger ribonucleoproteins (informosomes) and RNA-binding proteins. Mol Biol Rep, 5, 53−57.
  339. , A.S. (1994) Storage of messenger RNA in eukaryotes: envelopment with protein, translational barrier at 5' side, or conformational masking by 3' side? Mol Reprod Dev, 38, 107−117.
  340. Spohr, G., Kayibanda, B. and Scherrer, K. (1972) Polyribosome-bound and free-cytoplasmic-hemoglobin-messenger RNA in differentiating avian erythroblasts. Eur J Biochem, 31, 194−208.
  341. Stenina, O.I., Shaneyfelt, K.M. and DiCorleto, P.E. (2001) Thrombin induces the release of the Y-box protein dbpB from mRNA: a mechanism of transcriptional activation. Proc Natl Acad Sci USA, 98, 7277−7282.
  342. Stickeler, E., Fraser, S.D., Honig, A., Chen, A.L., Berget, S.M. and Cooper, T.A. (2001) The RNA binding protein YB-1 binds A/C-rich exon enhancers and stimulates splicing of the CD44 alternative exon v4. Embo J, 20, 3821−3830.
  343. Strasser, K. and Hurt, E. (2000) Yralp, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. Embo J, 19, 410−420.
  344. Strasser, K. and Hurt, E. (2001) Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yralp. Nature, 413, 648−652.
  345. Stutz, F., Bachi, A» Doerks, Π’., Braun, I.C., Seraphin, Π’., Wilm, M" Bork, P. and Izaurralde, E. (2000) REF, an evolutionary conserved family of hnRNP-like proteins, interacts with TAP/Mex67p and participates in mRNA nuclear export. Rna, 6, 638−650.
  346. Stutz, F. and Izaurralde, E. (2003) The interplay of nuclear mRNP assembly, mRNA surveillance and export. Trends Cell Biol, 13, 319−327.
  347. Svitkin, Y.V., Ovchinnikov, L.P., Dreyfuss, G. and Sonenberg, N. (1996) General RNA binding proteins render translation cap dependent. Embo /, 15, 7147−7155.
  348. Swamynathan, S.K., Nambiar, A. and Guntaka, R.V. (1998) Role of single-stranded DNA regions and Y-box proteins in transcriptional regulation of viral and cellular genes. FasebJ, 12, 515−522.
  349. Swanson, M.S. and Dreyfuss, G. (1988) Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol Cell Biol, 8,2237−2241.
  350. Tafuri, S.R. and Wolffe, A.P. (1990) Xenopus Y-box transcription factors: molecular cloning, functional analysis and developmental regulation. Proc Natl Acad Sci USA, 87, 9028−9032.
  351. Tafuri, S.R. and Wolffe, A.P. (1992) DNA binding, multimerization, and transcription stimulation by the Xenopus Y box proteins in vitro. New Biol, 4, 349−359.
  352. Tafuri, S.R., Familari, M. and Wolffe, A.P. (1993) A mouse Y box protein, MSY1, is associated with paternal mRNA in spermatocytes. J Biol Chem, 268, 12 213−12 220.
  353. Tan, W., Zolotukhin, A.S., Bear, J., Patenaude, D.J. and Felber, B.K. (2000) The mRNA export in Caenorhabditis elegans is mediated by Ce-NXF-1, an ortholog of human TAP/NXF and Saccharomyces cerevisiae Mex67p. Rna, 6, 1762−1772.
  354. Tanaka, Π’., Kondo, S., Iwasa, Y., Hiai, H. and Toyokuni, S. (2000) Expression of stress-response and cell proliferation genes in renal cell carcinoma induced by oxidative stress. Am J Pathol, 156, 2149−2157.
  355. Tarun, S.Z., Jr. and Sachs, A.B. (1995) A common function for mRNA 5' and 3' ends in translation initiation in yeast. Genes Dev, 9, 2997−3007.
  356. Tarun, S.Z., Jr. and Sachs, A.B. (1996) Association of the yeast poly (A) tail binding protein with translation initiation factor eIF-4G. Embo J, 15, 7168−7177.
  357. Tarun, S.Z., Jr., Wells, S.E., Deardorff, J.A. and Sachs, A.B. (1997) Translation initiation factor eIF4G mediates in vitro poly (A) tail-dependent translation. Proc Natl Acad Sci USA, 94, 9046−9051.
  358. Toh, S., Nakamura, Π’., Ohga, Π’., Koike, K., Uchiumi, Π’., Wada, M., Kuwano, M. and Kohno, K. (1998) Genomic organization of the human Y-box protein (YB-1) gene. Gene, 206, 93−97.
  359. Tomonaga, Π’., Michelotti, G.A., Libutti, D., Uy, A., Sauer, B. and Levens, D. (1998) Unrestraining genetic processes with a protein-DNA hinge. Mol Cell, 1, 759−764.
  360. Triqueneaux, G., Velten, M., Franzon, P., Dautry, F. and Jacquemin-Sablon, H. (1999) RNA binding specificity of Unr, a protein with five cold shock domains. Nucleic Acids Res, 21, 1926−1934.
  361. Tsanev, R.G. and Djondjurov, L.P. (1982) Ultrastructure of free ribonucleoprotein complexes in spread mammalian nuclei. J Cell Biol, 94, 662−666.
  362. Tucker, M., Staples, R.R., Valencia-Sanchez, M.A., Muhlrad, D. and Parker, R. (2002) Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae. Embo J, 21, 1427−1436.
  363. Uchida, N., Hoshino, S., Imataka, H., Sonenberg, N. and Katada, T. (2002) A novel role of the mammalian GSPT/eRF3 associating with poly (A)-binding protein in Cap/Po ly (A)-dependent translation. J Biol Chem, 277, 50 286−50 292.
  364. Uchiumi, Π’., Kohno, K., Tanimura, H., Matsuo, K., Sato, S., Uchida, Y. and Kuwano, M. (1993) Enhanced expression of the human multidrug resistance 1 gene in response to UV light irradiation. Cell Growth Differ, 4, 147−157.
  365. Uramoto, H., Izumi, H., Ise, Π’., Tada, M., Uchiumi, Π’., Kuwano, M., Yasumoto, K., Funa, K. and Kohno, K. (2002) p73 Interacts with c-Myc to regulate Y-box-binding protein-1 expression. J Biol Chem, 277, 31 694−31 702.
  366. Vasu, S.K. and Forbes, D.J. (2001) Nuclear pores and nuclear assembly. Curr Opin Cell Biol, 13, 363−375.
  367. Vazquez-Nin, G.H., Echeverria, O.M., Martin, Π’.Π•., Luhrmann, R. and Fakan, S. (1994) Immunocytochemical characterization of nuclear ribonucleoprotein fibrils in cells of the central nervous system of the rat. Eur J Cell Biol, 65, 291−297.
  368. Vincent, A., Goldenberg, S. and Scherrer, K. (1981) Comparisons of proteins associated with duck-globin mRNA and its polyadenylated segment in polyribosomal and repressed free messenger ribonucleoprotein complexes. Eur J Biochem, 114, 179−193.
  369. Visa, N., Alzhanova-Ericsson, A.T., Sun, X., Kiseleva, E., Bjorkroth, Π’., Wurtz, T. and Daneholt, B. (1996a) A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes. Cell, 84, 253−264.
  370. Visa, N., Izaurralde, E., Ferreira, J., Daneholt, B. and Mattaj, I.W. (1996b) A nuclear cap-binding complex binds Balbiani ring pre-mRNAtranscriptionally and accompanies the ribonucleoprotein particle during nuclear export. J Cell Biol, 133, 5−14.
  371. Wagenmakers, A.J., Reinders, R.J. and van Venrooij, W.J. (1980) Cross-linking of mRNA to proteins by irradiation of intact cells with ultraviolet light. Eur J Biochem, 112, 323−330.
  372. Wan, L., Kim, J.K., Pollard, V.W. and Dreyfuss, G. (2001) Mutational definition of RNA-binding and protein-protein interaction domains of heterogeneous nuclear RNP CI. J Biol Chem, 276, 7681−7688.
  373. Wang, M.Y., Cutler, M., Karimpour, I. and Kleene, K.C. (1992) Nucleotide sequence of a mouse testis poly (A) binding protein cDNA. Nucleic Acids Res, 20, 3519.
  374. Waxdal, M.J., Konigsberg, W.H., Henley, W.L. and Edelman, G.M. (1968) The covalent structure of a human gamma G-immunoglobulin. II. Isolation and characterization of the cyanogen bromide fragments. Biochemistry, 7, 1959−1966.
  375. Wei, C.C., Balasta, M.L., Ren, J. and Goss, D.J. (1998) Wheat germ poly (A) binding protein enhances the binding affinity of eukaryotic initiation factor 4 °F and (iso)4 °F for cap analogues. Biochemistry, 37, 1910−1916.
  376. Wells, S.E., Hillner, P.E., Vale, R.D. and Sachs, A.B. (1998) Circularization of mRNA by eukaryotic translation initiation factors. Mol Cell, 2, 135−140.
  377. Wilk, H.E., Werr, H., Friedrich, D" Kiltz, H.H. and Schafer, K.P. (1985) The core proteins of 35S hnRNP complexes. Characterization of nine different species. Eur J Biochem, 146, 71−81.
  378. Wilkie, G.S., Dickson, K.S. and Gray, N.K. (2003) Regulation of mRNA translation by 5'- and Π—'-UTR-binding factors. Trends Biochem Sci, 28, 182−188.
  379. Wilkinson, M.F. and Shyu, A.B. (2001) Multifunctional regulatory proteins that control gene expression in both the nucleus and the cytoplasm. Bioessays, 23, 775−787.
  380. Willimsky, G., Bang, H., Fischer, G. and Marahiel, M.A. (1992) Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures. J Bacteriol, 174, 6326−6335.
  381. , G. (1990) Cold shock and DNA binding. Nature, 344, 823−824.
  382. Wolffe, A.P., Tafuri, S., Ranjan, M. and Familari, M. (1992) The Y-box factors: a family of nucleic acid binding proteins conserved from Escherichia coli to man. New Biol, 4, 290−298.
  383. Wolffe, A.P. and Meric, F. (1996) Coupling transcription to translation: a novel site for the regulation of eukaryotic gene expression. Int J Biochem Cell Biol, 28, 247−257.
  384. Yang, L., Embree, L.J., Tsai, S. and Hickstein, D.D. (1998) Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing. J Biol Chem, 273, 2 776 127 764.
  385. Yenofsky, R., Bergmann, I. and Brawerman, G. (1982) Messenger RNA species partially in a repressed state in mouse sarcoma ascites cells. Proc Natl Acad Sci USA, 79, 5876−5880.
  386. Yokoyama, H., Harigae, H., Takahashi, S., Furuyama, K., Kaku, M., Yamamoto, M. and Sasaki, T. (2003) Regulation of YB-1 gene expression by GATA transcription factors. Biochem Biophys Res Commun, 303, 140−145.
  387. Yu, J., Hecht, N.B. and Schultz, R.M. (2002) RNA-binding properties and translation repression in vitro by germ cell-specific MSY2 protein. Biol Reprod, 67, 1093−1098.
  388. Zelus, B.D., Giebelhaus, D.H., Eib, D.W., Kenner, K.A. and Moon, R.T. (1989) Expression of the poly (A)-binding protein during development of Xenopus laevis. Mol Cell Biol, 9, 2756−2760.
  389. Zenklusen, D., Vinciguerra, P., Wyss, J.C. and Stutz, F. (2002) Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yralp and Sub2p by Hprlp. Mol Cell Biol, 22, 8241−8253.
Π—Π°ΠΏΠΎΠ»Π½ΠΈΡ‚ΡŒ Ρ„ΠΎΡ€ΠΌΡƒ Ρ‚Π΅ΠΊΡƒΡ‰Π΅ΠΉ Ρ€Π°Π±ΠΎΡ‚ΠΎΠΉ