Инициация трансляции эукариотических мРНК на эффективных лидерах: зависимость от факторов инициации и структуры лидера тема диссертации и автореферата по ВАК РФ 03.01.03, кандидат биологических наук Широких, Николай Эдуардович

  • Широких, Николай Эдуардович
  • кандидат биологических науккандидат биологических наук
  • 2010, Пущино
  • Специальность ВАК РФ03.01.03
  • Количество страниц 243
Широких, Николай Эдуардович. Инициация трансляции эукариотических мРНК на эффективных лидерах: зависимость от факторов инициации и структуры лидера: дис. кандидат биологических наук: 03.01.03 - Молекулярная биология. Пущино. 2010. 243 с.

Оглавление диссертации кандидат биологических наук Широких, Николай Эдуардович

Титульный лист.

Содержание.

Список условных сокращений.б

Глава 1. Введение.

Глава 2. Обзор литературы.'.

2.1. Контроль экспрессии генов и биосинтез белка.

2.1.1. Центральная догма молекулярной биологии.

2.1.2'. Основные способы посттранскрипционной регуляции экспрессии генов в цитоплазме эукариот.

2.1.3. Регуляция экспрессии генов во время трансляции мРНКу эукариот.

2.2. Инициация трансляции у эукариот.

2.2.1. Отличие инициации от других этапов трансляции мРНК.

2.2.2. Инициация трансляции у эукариотических организмов: ключевые участники процесса.

2.2.3. Общепринятая модель инициации трансляции мРНК клеточного происхождения у эукариот.

2.3. Задачи исследования.

Глава 3. Материалы исследования.

3.1. Оборудование.

3.2. Химические реагенты.

3.3. Ферменты.

3.4. Буферные растворы и микробиологические среды.

3.5. Генетические конструкции.

3.6. ДНК-олигонуклеотиды.

3.7. Штаммы клеток.

3.8. Программные инструменты.

Глава 4. Методы исследования.

4.1. Стандартные методики.

4.2. Получение компетентных клеток Escherichia coil штаммов DH5a и BL21(DE3).

4.3. Трансформация компетентных клеток Escherichia coli плазмидными векторами.

4.4. Электрофорез нуклеиновых кислот в неденатурирующем агарозном геле.

4.5. Очистка ДНК-плазмид.

4.6. Очистка ДНК-плазмид без использования РНКаз.

4.7. Очистка ДНК-плазмид от низкополимерных нуклеиновых кислот.

4.8. Препаративная рестрикция плазмид и фрагментов ДНК.

4.9. Препаративное разделение и очистка фрагментов ДНК разной длины с помощью электрофореза в неденатурирующем агарозном геле.

4.10. Отщепление 5'-концевых фосфатных групп от фрагментов ДНК после их расщепления рестриктазами.

4.11. Отжиг комплементарных участков цепей синтетических олигонуклеотидов для последующего встраивания двуцепочечного фрагмента ДНК в плазмидный вектор с помощъюлигирования.

4.12. Амплификация фрагментов ДНК с помощью полимеразой цепной реакции.

4.13. Фосфорилирование 5'-концов двуцепочечных фрагментов ДНК с помощью полинуклеотидкиназы.

4.14. Лигирование фрагментов ДНК.

4.15. Секвенирование плазмид и фрагментов ДНК.

4.16. Конструирование плазмиды рп50.

4.17. Конструирование плазмиды pTZA25Luc.

4.18. Конструирование плазмид pTZMlluc, pTZM2Luc, pTZM3Luc.

4.19. Конструирование плазмиды pTZOX2FRLuc.

4.20. In vitro транскрипция.

4.21. Осаждение фрагментов РНК длиной от 20 нт с минимальным соосаждением свободных нуклеотидов.

4.22. Гель-фильтрация макромолекул РНК или ДНК для очистки от низкомолекулярных примесей.

4.23. Гель-фильтрационное разделение молекул РНК.

4.24. Электрофоретическое разделение нуклеиновых кислот в денатурирующем полиакриламидном геле.

4.25. Неполный щелочной гидролиз РНК.

4.26. Препаративное электрофоретическое разделение нуклеиновых кислот в денатурирующем полиакриламидном геле.:.

4.27. Электрофорез РНК в агарозном геле в солевых условиях, близких к

• физиологическим.

4.28. Модификация РНК диметилсульфатом.

4.29. Модификация РНК диэтилпирокарбонатом.

4.30. Расщепление РНКРНКазой VI.

4.31. Расщепление РНКРНКазой А.

4.32. Обратная транскрипция РНК после частичной модификации или расщепления.

4.33. Капиллярный электрофорез, считывание флуоресценции и анализ сигнала от разделенных кДНК-транскриптов модифицированной или расщепленной РНК.

4.34. Аналитическое ультрацентрифугирование водных растворов РНК.

4.35. Тепловое плавление РНК, измеренное по изменению абсорбции света на длине волны 258 нм.

4.36. ЯМР-спектрометрия водных растворов РНК.

4.37. Получениелизата ретикулоцитов кролика.

4.38. Удаление эндогенных мРНК из лизата ретикулоцитов кролика с помощью обработки микрококковой нуклеазой.

4.39. In vitro трансляция.

4.40. Осаждение фракции белков из реакционной смеси для in vitro трансляции, нерастворимой в трихлоруксусной кислоте.

4.41. Подсчет количества радиоактивности во фракции белков трансляционной смеси, осажденных на бумаге трихлоруксусной кислотой.

4.42. Ионообменная хроматография белков на колонке, содержащей диэтиламиноэтил-целлюлозу.

4.43. Ионообменная хроматография белков на колонке, содержащей фосфоцеллюлозу.

4.44. Ионообменная хроматография белков на колонках Mono-Q и Mono-S.

4.45. Аффинная очистка белков на колонке с Ni-NTA агарозой.

4.46. Аффинная очистка белков на колонке с 7тСТР-сефарозой.

4.47. Концентрирование белков, рибосом и их субъединиц ультрафильтрацией.

4.48. Диализ рибосом, субъединиц рибосом и белков.

4.49. Осаждение белков ацетоном в целях их концентрирования и удаления ионов К+ из раствора.

4.50. Электрофоретическое разделение белков в денатурирующем полиакриламидном геле.

4.51. Выделение факторов инициации трансляции eIF2, eIF3, eIF3-eIF4F из лизата ретикулоцитов кролика.

4.52. Выделение субъединиц рибосом из лизата ретикулоцитов кролика.

4.53. Выделение мРНКр-глобина из лизата ретикулоцитов кролика.

4.54. Экспрессия рекомбинантных плазмид, кодирующих факторы инициации трансляции млекопитающих и инициаторную аминоацил-тРНК синтетазу Escherichia coli, в клетках Escherichia coli, и очистка соответствующих белков.

4.55. Подсчет радиоактивности в срт в водных растворах, содержащих радиоактивно меченые белки или нуклеиновые кислоты.

4.56. Визуализация и оценка радиоактивности изотопов в полиакриламидном геле после электрофоретического разделения белков или нуклеиновых кислот.

4.57. Аминоацилирование инициаторной тРНК млекопитающих рекомбинантной аминоацил-тРНК синтетазой Escherichia coli.

4.58. Аминоацилирование тотальной тРНКпо Met, Val, His и Leu.

4.59. Сборка инициаторных комплексов эукариот из очищенных компонентов in vitro.

4.60. Сборка инициаторных комплексов эукариот в нефракционированном лизате ретикулоцитов кролика, обработанном микрококковой нуклеазой, in vitro.

4.61. Реакция удлиненияпептида в мРНК-рибосомных комплексах эукариот, собранных из очищенных компонентов in vitro.

4.62. Сборка и очистка пре-терминационного комплекса трансляции эукариот из очищенных компонентов in vitro.

4.63. Реакция терминации трансляции в мРНК-рибосомных комплексах эукариот, собранных из очищенных компонентов in vitro.

4.64. Реакция ингибированияудлинения праймера мРНК-рибосомными комплексами эукариот (тупринтинг).

4.65. Анализ флуоресцентно меченых кДНК, полученных в реакции тупринтинга, капиллярным электрофорезом на автоматическом секвенаторе.

Глава 5. Результаты и обсуждение результатов работы.

5.1. Улучшенный метод ингибирования удлинения праймера рибосомными комплексами на мРНК (тупринтинг).

5.1.1. Основы метода ингибирования удлинения праймера.

5.1.2. Стандартный метод ингибирования удлинения праймера рибосомными комплексами на мРНК.

5.1.3. Метод ингибирования удлинения праймера рибосомными комплексами на мРНК с использованием флуоресцентной метки и капиллярного электрофореза.

5.1.4. Оптимизация условий обратной транскрипции для реакции тупринтинга.

5.1.5. мРНК-рибосомные комплексы, которые могут быть исследованы методом ингибирования удлинения праймера.

5.1.6. Обнаружение рибосомных комплексов на мРНК.

5.1.7. Анализ электрофореграмм, полученных методом тупринтинга с флуоресцентной меткой.

5.1.8. Оптимизация выхода инициаторных мРНК-рибосомных комплексов для реакции тупринтинга.

5.1.9. Идентификация мРНК-рибосомных комплексов методом тупринтинга с флуоресцентной меткой.

5.1.10. Расчет эффективности реакций инициации, элонгации и терминации трансляции методом флуоресцентного тупринтинга.

5.1.11. Обнаружение нескольких мест сборки мРНК-рибосомных комплексов в одной и той же реакционной смеси с помощью метода тупринтинга.

5.1.12. Общая характеристика улучшенного метода тупринтинга с применением флуоресцентной метки и капиллярного электрофореза.

Рекомендованный список диссертаций по специальности «Молекулярная биология», 03.01.03 шифр ВАК

Заключение диссертации по теме «Молекулярная биология», Широких, Николай Эдуардович

Выводы:

1. Методами аналитического центрифугирования и теплового плавления показано, что РНК с последовательностью омега-лидера геномной РНК вируса табачной мозаики обладает коэффициентом седиментации, характерным для компактно уложенных РНК, и имеет большую величину гиперхромного эффекта при плавлении, сопровождающимся кооперативным структурным переходом в области высоких температур;

2. Методами химического и энзиматического тестирования, а также методом ядерного магнитного резонанса показано, что центральная (САА)„-содержащая часть омега-РНК не модифицируется агентами, действующими на одноцепочечную РНК, а вся структура омега-РНК формирует укладку на основе неканонических взаимодействий нуклеотидов;

3. Методом тупринтинга показано, что для сборки инициаторного 48Б комплекса на омега-РНК не требуется факторов инициации трансляции еШ4А и еШ4Р, ответственных за АТФ-зависимое сканирование;

4. Сделано предположение о возможном участии структуры омега-последовательности РНК в ее функциональной активности как универсального лидера, усиливающего трансляцию мРНК.

Глава 6. Резюме результатов работы

Согласно современным представлениям, инициация трансляции на мРНК у эукариот происходит по одному из двух возможных сценариев. В случае клеточных мРНК, трансляция начинается кэп-зависимо, с последующим АТФ-зависимым, 5'—>3' направленным сканированием 5'-нетранслируемой области до нахождения первого стартового кодона в определенном нуклеотидном контексте. В противоположность этому, на мРНК некоторых вирусов трансляция может начинаться вдалеке от 5'-конца мРНК благодаря непосредственному или опосредованному специфическому связыванию 40Б субъединицы рибосом со специальным структурным модулем в составе мРНК — сайте внутренней посадки рибосом. В этой работе мы изучили механизм инициации трансляции на двух разных лидерных последовательностях мРНК, известных свой способностью обеспечивать эффективную кэп-независимую инициацию трансляции. Как было показано ранее, 5'-поли(А) лидерная последовательность, характерная для мРНК осповирусов, и омега-последовательность 5'-нетранслируеммой области РНК вируса табачной мозаики могут кэп-независимо усиливать трансляцию чужеродных кодирующих частей РНК в разных клетках и системах бесклеточной трансляции. В то же время, обе этих лидерных последовательности не содержат сайтов внутренней посадки рибосом. Трансляционные свойства 5'-поли(А) и омега-лидерных последовательностей плохо описываются имеющейся моделью эукариотической инициации трансляции и могут быть объяснены реализацией иного механизма инициации трансляции на них.

Чтобы выяснить механизм инициации трансляции на 5'-поли(А) и омега- лидерных последовательностях, мы исследовали зависимость эффективности инициации трансляции на мРНК, содержавшей эти последовательности, от набора факторов инициации трансляции в системе, собранной из отдельных очищенных компонентов. Для того, чтобы получить данные этой зависимости, мы применили метод ингибирования удлинения праймера мРНК-рибосомными комплексами (тупринтинг) — метод, ранее хорошо зарекомендовавший себя для решения подобных задач. Нами был создан усовершенствованный вариант метода тупринтинга, в котором для обнаружения и подсчета кДНК продуктов обратной транскрипции используется флуоресцентная метка, а для их разделения — капиллярный электрофорез. Усовершенствованный метод тупринтинга позволяет обнаруживать и идентифицировать мРНК-рибосомные комплексы на всех стадиях трансляции (инициации, элонгации и терминации), а также быстро и точно подсчитывать количество обнаруженных мРПК-рибосомных комплексов и эффективность соответствующих стадий трансляции. Усовершенствованный метод тупринтинга имеет уникальные преимущества перед обычным вариантом метода с использованием, радиоактивных изотопов: благодаря возможности применять флуорофоры с разными спектральными' характеристиками, метод позволяет исследовать несколько мест сборки мРНК-рибосомных комплексов в одной и той же реакционной смеси независимо друг от друга.

Некэпированные мРНК с 5'-поли(А) и омега-лидерами продемонстрировали полную-независимость инициации трансляции на них от факторов сканирования — белков е1Р4А, еШ4В и е№4Р. Известно, что для типичной клеточной мРНК, например природной бета-глобиновой мРНК, требуется полный набор факторов инициации трансляции, включающий в себя белки еШ1, сШ1А, с1¥2, еШЗ, е1Р4А, е№4В и е1Р4Р, несмотря на отсутствие в лидере бета-глобиновой мРНК стабильных вторичных структур РНК. Эффективная инициация трансляции на мРНК с 5'-поли(А) и омега-лидерами без белков еШ4А/Р подразумевает энергонезависимый механизм инициации трансляции, в котором не используется энергия гидролиза АТФ. Так как ранее в нашей лаборатории было показано, что эффективность инициации трансляции не мРНК с поли(А)-лидером прямо зависит от длины поли(А)-лидера, то присоединение инициирующей малой рибосомной субъединицы должно происходить в этом случае по всей длине лидерной последовательности, а не только зависимо от 5-конца мРНК. Какой механизм может обеспечивать нахождение стартового кодона в этом случае после присоединения 40Б субъединицы рибосом к последовательности лидера мРНК? Механизм энергонезависимой одномерной диффузии был ранее предложен и подтвержден для объяснения нахождения стартового кодона, находящегося в составе многоцистронной мРНК прокариот, ЗОБ рибосомными субъединицами после терминации трансляции на предшествующем цистроне. По-видимому, такой же механизм «бесфазного блуждания» малых рибосомных субъединиц по лидерной последовательности мРНК реализуется у эукариот в случае е1Р4А/Р независимой инициации трансляции. Альтернативный механизм инициации трансляции, обнаруженный нами на мРНК с 5'-поли(А) и омега-лидерами, состоит из следующих этапов: (1) неспецифическое присоединение инициирующей малой рибосомной субъединицы к цепи лидерной последовательности мРНК, (2) ненаправленное, энергонезависимое диффузионное движение 40Б субъединицы рибосом вдоль цепи лидера, (3) фиксация на стартовом кодоне, когда нужный триплет мРНК в правильном нуклеотидном окружении окажется в Р-сайте рибосомы. Обнаруженный нами механизм инициации трансляции имеет значительные отличия как от канонической инициации трансляции посредством 5-концевой кэп-структуры мРНК и сканирования, так и от инициации трансляции на сайтах внутренней посадки рибосом. По-видимому, целесообразно выделение такого механизма инициации трансляции как отдельностоящего, третьего пути в существующей модели инициации трансляции у эукариот.

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Эффективная инициация1 трансляции на мРНК с поли(А)-лидером- оказалась возможной без самого большого мультисубъединичного белка инициации трансляции — eIF3. Это уникальное свойство поли(А)-лидера: эффективная инициация трансляции без фактора инициации eIF3 известна только для ограниченного числа' вирусных сайтов« внутренней' посадки рибосом, и не наблюдается для других лидерных последовательностей, не содержащих сайты внутренней посадки рибосом. Несмотря на размер белка, функциональная активность eIF3 остается наименее точно обозначенной из всех основных факторов инициации трансляции. Независимость эффективности инициации трансляции на мРНК с поли(А)-лидером от фактора инициации eIF3 вместе с отсутствием структур сайтов внутренней посадки рибосом в этой последовательности позволила нам прояснить функцию этого белка в инициации трансляции. С помощью метода тупринтинга мы показали, что завершение инициации трансляции, включающее в себя гидролиз е1Р2-связанного ГТФ в составе 48S инициаторного комплекса, выход eIF2-GDP из состава инициаторного комплекса, присоединение eIF5B-GTP к инициаторному комплексу, гидролиз eIF5B-связанного ГТФ, отсоединение CIF5B-GDP и присоединение 60S рибосомных субъединиц с образованием 80S инициаторного комплекса, способного к элонгации, происходят без участия белка eIF3 с такой же эффективностью, как и в присутствии eIF3. Согласно данным других исследователей, отсоединение eIF3 от инициаторного комплекса происходило преимущественно после образования 80S инициаторного комплекса, что косвенно предполагало участие eIF3 во всех стадиях инициации трансляции. Данные, полученные нами, свидетельствуют о функциональной активности eIF3, необходимой только во время присоединения рибосом к мРНК, сканирования и образования инициаторного 48S комплекса. Чем могут объясняться уникальные трансляционные свойства поли(А)-лидеров мРНК, обеспечивающего е1РЗ-независимую инициацию трансляции? Возможно, эти свойства связаны со структурными особенностями РНК с поли(А)-последовательностями. Известно, что полирибонуклеотид (А)„ в растворе при физиологических условиях формирует стабильную одноцепочечную спираль, конформационно близкую к A-форме спирали РНК. В составе прокариотических инициаторных комплексов, структура которых детально изучена, 5'-лидерная часть мРНК формирует примерно один виток одноцепочечной А-спирали, стабилизированный в этом случае взаимодействиями с анти-Шайн-Дальгарно последовательностью pPHK. eIF3 располагается на эукариотической рибосоме в области 5'-лидерной части связанной мРНК, находящейся непосредственно перед стартовым' кодоном. Возможно, в случае гетеронуклеотидных последовательностей в лидерной части мРНК, eIF3 необходим для придания им нужной для связывания с 40S субъединицей рибосом конформации. поли(А)-лидерные последовательности обладают такой конформацией сами

180 по себе, и поэтому еШЗ не требуется для^ эффективной инициации трансляции» на них. Указанная вероятная функция еШЗ характеризует его активность на рибосоме как аналогичную функциям анти-Шайн-Дальгарно последовательности рРНК или белка Б1 у эубактерий и архей.

Уникальность укладки цепи РНК в полинуклеотиде, содержащем омега-последовательность, может способствовать образованиюь обособленной' и стабильной структуры в составе полноразмерной РНК ВТМ. Известно, что белок оболочки тобамовирусов взаимодействует с развернутой одноцепочечной конформацией РНК. Таким образом, тенденция омега-последовательности к формированию стабильной структуры должна уменьшать сродство белка оболочки ВТМ к этой последовательности, что может объяснять начало 5'-проксимальной разборки вириона ВТМ при его попадании в клетку, которое жизненно необходимо для репликации этого вируса. Здесь уместна аналогия с 3'-частью РНК ВТМ, для которой ранее было показано образование стабильных тРНК-подобных и псевдоузловых структур. Другими исследователями было показано, что 3'-проксимальные структуры РНК ВТМ необходимы для успешной репликации этого вируса в клетках хозяина. Возможно, что наличие способности к образованию этих структур в З1-концевой области РНК ВТМ также способствует началу репликации благодаря пониженному сродству белка оболочки к этой области РНК.

Несмотря на наличие стабильной вторичной и третичной структуры, омега-лидер обеспечивает эффективную кэп-независимую инициацию трансляции. Возможно, трехмерная конфигурация омега-РНК способствует облегченному присоединению 40Б субъединиц к этому лидеру и формирование 48Б инициаторного комплекса с высоким выходом без факторов сканирования — так же, как одноцепочечная спираль поли(А)-РНК, вероятно, обеспечивает еШЗ-независимую инициацию трансляции. Вместе с этим, структура омега-РНК ВТМ не обеспечивает высокоаффинного (и специфического) сродства этой последовательности к рибосомам или факторам инициации трансляции, как это имеет место в случае инициации трансляции на сайтах внутренней посадки рибосом. Эти факты приводят нас к заключению о том, что инициация трансляции на омега-лидере ВТМ может происходить по альтернативному пути, отличному от кэп-зависимого сканирования и инициации на сайтах внутренней посадки рибосом.

1. Разработан усовершенствованный метод ингибирования удлинения праймера мРНК-рибосомными комплексами (тупринтинг), в котором для мечения продуктов реакции обратной транскрипции используются флуоресцентные группы, а для их разделения применяется капиллярный электрофорез. Показано, что усовершенствованным методом тупринтинга можно обнаруживать, идентифицировать и количественно подсчитывать мРНК-рибосомные комплексы на всех стадиях трансляции: инициации, элонгации и терминации.

2. Методом тупринтинга показано, что поли(А)-лидер, характерный для мРНК осповирусов, обеспечивает эффективную инициацию трансляции на рекомбинантной мРНК без факторов инициации е1Р4А, е1Р4В и е1Р4Р, ответственных за АТФ-зависимое сканирование, а также без белка е1РЗ. Методом тупринтинга на мРНК с поли(А)-лидером показано также, что фактор инициации е1РЗ не требуется для объединения субъединиц рибосом при инициации трансляции.

3. Методом тупринтинга показано, что для сборки инициаторного 48Б комплекса на омега-лидере вируса табачной мозаики не требуется факторов инициации трансляции еШ4А и е1Р4Р, ответственных за АТФ-зависимое сканирование, но требуется е№3.

4. Изучена структура омега-лидера РНК вируса табачной мозаики. а) Методами аналитического центрифугирования и теплового плавления показано, что РНК с последовательностью омега-лидера геномной РНК вируса табачной мозаики обладает коэффициентом седиментации, характерным для компактно уложенных РНК и имеет большую величину гиперхромного эффекта при плавлении, сопровождающимся кооперативным структурным переходом в области высоких температур б) Методами химического и энзиматического тестирования, а также методом ядерного магнитного резонанса, показано, что центральная (САА)„-содержащая часть омега-РНК не модифицируется агентами, действующими на одноцепочечную РНК, а вся структура омега-РНК формирует укладку на основе неканонических взаимодействий нуклеотидов.

5. Предложена модель альтернативного механизма инициации трансляции на А-обогащенных лидерных последовательностях эукариотических мРНК. Модель предполагает посадку инициирующей субъединицы рибосом в произвольном месте лидерной последовательности мРНК и ее последующее энергонезависимое диффузионное движение («бесфазное блуждание») по цепи мРНК.

5.3.9. Заключение

Методами скоростного ультрацентрифугирования, температурного плавления и ядерного магнитного резонанса мы показали, что РНК, содержащая. омега-РНК ВТМ, имеет коэффициент седиментации компактно свернутой РНК и кооперативно плавится при высокой температуре. Следовательно, эта РНК формирует стабильную и компактную структуру в растворе при физиологических условиях. Омега-РНК — известный

174 универсальный усилитель эффективности трансляции открытых рамок считывания, белков. Основным доводом исследователей, изучавших ранее эффект усиления трансляции мРНК омега-лидером, было объяснение эффективной инициации трансляции омега-лидером через презумпцию неструктурированности этой РНК. Неструктурированность (или низкая структурированность) омега-РНК подтверждалась в первую - очередь невозможностью предсказания ее вторичной структуры стандартными методами компьютерного моделирования. На основе природной последовательности' омега-РНК другими исследователями ранее был предложен эффективный «неструктурированный» синтетический лидер РНК — последовательность (САА)щ. Компактность и температурная стабильность (CAA)i9-PHK, определенные нами, не позволяют идентифицировать (CAA) 19 РНК как неструктурированную РНК.

Методами химического и энзиматического тестирования, а также методом ядерного магнитного резонанса, мы показали, что центральная (САА)„-содержащая часть омега-РНК не модифицируется агентами, действующими на одноцепочечную РНК, а вся структура омега-РНК формирует укладку на основе неканонических взаимодействий нуклеотидов. Следовательно, омега-РНК имеет стабильную вторичную структуру не уотсон-криковского типа. Эта структура может быть основана на структуре тройной спирали (CAA) 19. На основе данных о расщеплении коротких участков в З'-проксимальной (А,и)„-содержащей области омега-РНК РНКазой VI, высоком коэффициенте седиментации этой РНК и консервативности последовательностей в 3'-(А,и)„-области омега-РНК, мы предположили, что 3'-проксимальные (А,^„-последовательности омега-РНК могут принимать участие в третичных взаимодействиях в составе структуры этой РНК.

Методами скоростного ульграцентрифугирования и температурного плавления мы исследовали гидродинамические свойства РНК, содержавших последовательности омега-РНК, измененные в местах, которые по нашим предположениям являлись ключевыми для формирования стабильной и компактной структуры этой РНК. В частности, РНК с заменами трех аденинов на три цитозина в составе (САА)„-содержащей части омега-последовательности обладала существенно более низким коэффициентом седиментации, а также меньшим гипохромизм и кооперативностью структурного перехода при плавлении, чем исходная омега-РНК. Замена трех аденинов на три цитозина была предложена для омега-РНК как воздействие, способное дестабилизировать возможную тройную спираль РНК в этой молекуле. Таким образом, этот результат является доводом в пользу существования тройной спирали предложенного типа в омега-РНК. РНК, в которой консервативные 3'-проксимальные (А,^„-последовательности омега-РНК были замещены на (G,C)„-последовательности, также показала снижение коэффициента седиментации, (потерю

175 компактности) и практически полное отсутствие кооперативности плавления и уменьшенный гиперхромный эффект (потерю стабильности). Следовательно, 3'-проксимальные (А,^„-последовательности омега-РНК принимают участие в стабилизации и компактизации общей третичной укладки этой РНК.

Методом тупринтинга мы показали, что для сборки инициаторного 48Б комплекса на омега-РНК не требуется факторов инициации трансляции, ответственных за АТФ-зависимое сканирование: е1Р4А/Р. Так как омега-РНК обеспечивает эффективную кэп-независимую инициацию трансляции без АТФ-зависимого сканирования, но не содержит явных сайтов внутренней посадки рибосом, этот лидер инициирует трансляцию по альтернативному механизму. Так же, как и в случае поли(А)-лидеров РНК, на РНК с 5'-омега-послсдовательностью возможно неспецифическое присоединение инициирующей рибосомной субъединицы к последовательности лидера, с последующим «бесфазным блужданием» малой субъединицы рибосом по цепи лидера до нахождения инициаторного кодона. Способность формировать 48Б комплекс без АТФ была показана ранее другими исследователями для (САА)19-лидера РНК - что объяснялось неструктурированной природой и одноцепочечной конфигурацией (САА)19-РНК ([109]). В то же время хорошо известно, что инициация трансляции на лидере мРНК белка бета-глобина требует участия факторов АТФ-зависимого сканирования ([109, 167]), и методами энзиматического тестирования структуры РНК было показано, что РНК с последовательностью лидера бета-глобиновой мРНК находится в растворе в преимущественно неструктурированном виде [338, 846]. Следовательно, именно структурные особенности омега-последовательности могут быть ответственны за эффективную инициацию трансляции на мРНК с омега-ли дером.

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743. Я благодарю С.Ч. Агаларова за крайне важное для выполнения этой работы сотрудничество, массу полезных советов и обсуждений.

744. Искренне благодарю Л.П. Гаврилову и В.Д. Васильева за советы, сотрудничество и оказанную чрезвычайно теплую и незаменимую моральную поддержу.

745. Я благодарю О.М. Алехину и К.С. Василенко за плодотворные дискуссии, многочисленные случаи взаимовыручки, которыми я им обязан, сотрудничество и неизбывно доброжелательное общение.

746. Выражаю глубочайшие благодарность и признательность А.Г. Рязанову за бесценные советы, обсуждения и реактивы, без которых данной работы просто не было бы.

747. Я благодарю мою жену и всех близких родственников, которые с пониманием отнеслись к процессу написания данной работы и всемерно помогали мне.

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