Генетический контроль терминации трансляции у эукариот тема диссертации и автореферата по ВАК РФ 03.00.15, доктор биологических наук Журавлева, Галина Анатольевна

• Журавлева, Галина Анатольевна
• доктор биологических наук
• 2007

Оглавление диссертации доктор биологических наук Журавлева, Галина Анатольевна

СПИСОК СОКРАЩЕНИЙ

Глава 1. ЭВОЛЮЦИОННАЯ КОНСЕРВАТИВНОСТЬ

ФАКТОРОВ ТРАНСЛЯЦИИ ЭУКАРИОТ (ВВЕДЕНИЕ)

Глава 2. МАТЕРИАЛЫ И МЕТОДЫ

2.1. Штаммы

2.2. Плазмиды

2.2.1. Плазмиды для двугибридной системы

2.2.2. Плазмиды для аффинной хроматографии

2.2.3. Плазмиды серии pYX

2.2.4. Плазмиды, содержащие мутантные аллели генов 33 SUP45 и SUP

2.3. Секвенирование

2.4. Среды и условия культивирования

2.5. Молекулярно-генетические методы

2.5.1. Получение мутантов по генам SUP35 и SUP

2.5.2. Количественная оценка стабильности плазмид

2.5.3. Двугибридная система

2.6. Молекулярно-биологические и биохимические 40 методы

2.6.1. Скрининг библиотеки кДНК с помощью гибридизации

2.6.2. Скрининг библиотек кДНК с помощью двугибридной 41 системы

2.6.3. Количественная характеристика нонсенс-супрессии

2.6.4. Нозерн-гибридизация

2.6.5. Антитела

2.6.6. Иммуноблотинг

2.6.7. Детекция взаимодействия белков

2.7. Компьютерные и статистические методы

Глава 3. Белок eRF3 - эукариотический фактор терминации трансляции 2 класса

3.1. История изучения терминации трансляции у про- и эукариот (обзор литературы)

3.1.1. Нонсенс-супрессия у прокариот

3.1.2. Нонсенс-супрессия у дрожжей S. cerevisiae

3.1.2.1. Кодон-специфическая супрессия

3.1.2.2. Омнипотентная супрессия. Идентификация генов 55 SUP45 и SUP

3.1.2.3. Взаимодействие рецессивных омнипотентных супрессоров с кодон-специфичными супрессорами 3.1.2.4. Модификаторы нонсенс-супрессии, аллосупрессоры и 58 антисупрессоры

3.1.3. Белки 8ир45 и 8ир35 участвуют в контроле точности 61 трансляции

3.1.4. Гипотезы о белках, участвующих в терминации 65 трансляции у эукариот

3.2. Изоляция структурного гена Хепорш 1аехЬ, 66 гомологичного гену 31/Р35 дрожжей

3.2.1. Скрининг библиотеки кДНК X. \aevis

3.2.2. Сравнение С-терминальных доменов белков, 68 гомологичных 8ир35 из разных видов

3.2.3. Комплементация мутации зир35-21^) белком 8ир35-С 69 X. \aevis

3.2.4. Идентификация фактора терминации еИРЗ

3.3. Во взаимодействии с белком еДОЗ участвует С- 72 терминальный домен белка еВД!

3.4. Эволюционная консервативность взаимодействия 75 факторов терминации трансляции еШ^ и еДОЗ

3.5. Факторы терминации трансляции эукариот еЫП и 77 еШ?3 (обсуждение)

3.5.1. Терминация трансляции у эукариот

3.5.2. Фактор терминации трансляции еШЛ

3.5.3. Роль рибосомы в декодировании

3.5.4. Фактор терминации трансляции еЮ^

3.5.5. Терминация трансляции и молекулярная мимикрия

Глава 4. ИЗУЧЕНИЕ ФУНКЦИОНАЛЬНОЙ

ГОМОЛОГИИ БЕЛКОВ СЕМЕЙСТВА eRF3 ВЫСШИХ ЭУКАРИОТ (Н. sapiens, X. laevis, М. musculus) В КЛЕТКАХ ДРОЖЖЕЙ

4.1. Подсемейство факторов терминации eRF3 (Обзор 91 литературы)

4.2. Функциональное замещение дрожжевого фактора 95 терминации eRF3 белком mGSPT2 М. musculus

4.3. Делеционный анализ генов mGSPTl и mGSPT

4.4. Роль N-терминального домена в функционировании фактора терминации eRF

4.5. Взаимодействие белков GSPT1 и GSPT2 с белком 105 eRFl

4.6. Белок Hbsl S. cerevisiae филогенетически, но не 107 функционально, родственен белку eRF

4.6.1. Филогенетический анализ белков Hbsl S. cerevisiae и 107 eRFS Н. sapiens

4.6.2. Белки Hbsl и eRFS не способны функционировать в 108 качестве факторов терминации в клетках дрожжей

4.6.3. Белок Hbsl не взаимодействует с факторами 109 терминации eRF3 и eRFl

4.7. Консервативность фактора терминации 110 трансляции eRF3 у эукариот (Обсуждение)

4.7.1. Гены, кодирующие eRF3, у разных организмов

4.7.2. Структурная организация белка eRF

4.7.2.1. N-терминальный домен белка eRF

4.7.2.2. М- домен белка eRF

4.7.2.3. С-терминальный домен белка eRF

4.7.3. Функциональная гомология белков подсемейства eRF

4.7.4. Роль белка Hbsl в трансляции

Глава 5. ИСПОЛЬЗОВАНИЕ МУТАНТОВ ПО ГЕНАМ

SUP45VLSUP35 ДЛЯ ИЗУЧЕНИЯ СОБЫТИЙ, ПРОИСХОДЯЩИХ ПРИ ТЕРМИНАЦИИ ТРАНСЛЯЦИИ

5.1. Мутации sup45 и sup35 и их плейотропные 131 эффекты (обзор литературы)

5.1.1. Омнипотентная супрессия

5.1.2. Супрессия сдвигов считывания

5.1.3. Чувствительность к антибиотикам

5.1.4. Температурочувствительность

5.1.5. Осмочувствительность

5.1.6. Влияние мутаций sup35 и sup45 на функционирование 133 митохондрий

5.1.7. Влияние мутаций sup35 и sup45 на клеточный цикл

5.1.8. Фенотшшческое проявление фактора [PSf]

5.2. Использование мутантов по гену SUP45 для 139 изучения событий, происходящих при терминации трансляции

5.2.1. Мутации sup45, отобранные по эффекту супрессии 139 мутаций his7-l (UAA) и Iys9-A21 (UAA)

5.2.2. Нонсенс-мутации (sup45-n) в жизненно-важном гене

5.2.3. Мутации sup45-n приводят к трансляции стоп- 145 кодонов, как значащих

5.2.4. Жизнеспособность различных по происхождению 147 штаммов, содержащих мутации sup45-n

5.2.5. Мутации sup45-n нарушают жизнеспособность 151 аскоспор в мейозе

5.2.6. Присутствие аллели дикого типа гена SUP45 154 нарушает трансляцию нонсенс-кодонов

5.2.7. Миссенс-мутации в гене SUP

5.2.7.1. Фенотипическая характеристика миссенс-мутаций 157 в гене SUP

5.2.7.2. Миссенс-мутации в гене SUP45 не влияют 158 на количество белка eRFl

5.2.7.3. Большинство миссенс-мутаций в гене SUP45 159 не влияет на взаимодействие мутантных белков eRFl с бежом eRF3 в двугибридной системе

5.3. Использование мутантов по гену SUP35 для 160 изучения событий, происходящих при терминации трансляции

5.3.1. Характеристика белка eRF3 у мутантов по гену SUP

5.3.2. Секвенирование мутаций sup

5.3.3. Нонсенс-мутации в гене SUP35 (sup35-n) 167 не влияют на количество мРНК SUP

5.3.4. Мутации sup35-n не приводят к летальности в 168 отсутствие мутантной тРНК

5.3.5. Нонсенс-мутации в генах SUP45 и SUP35 не приводят к 170 уменьшению содержания белков eRFl и eRF3, соответственно

5.3.6. Миссенс-мутации в гене SUP35 не приводят к 172 нарушению взаимодействия с белком eRFl

5.4. Увеличение уровня тРНК у мутантов по факторам 173 терминации eRFl и eRF

5.4.1. Жизнеспособность нонсенс-мутантов по генам SUP45 173 и SUP35 увеличивается с увеличением числагенераций в условиях отбора

5.4.2. Нонсенс-мутанты по гену SUP45 характеризуются 176 повышенным содержанием тРНК

5.4.3. Количество тРНК в штаммах, несущих мутации sup

5.5. Мутации в генах SUP45 и SUP35 (Обсуждение)

5.5.1. Типы мутаций, возникающих в генах SUP45 и SUP

5.5.2. Миссенс-мутации в генах SUP45 и SUP

5.5.2.1. Миссенс-мутации в гене SUP

5.5.2.2. Миссенс-мутации в гене SUP

5.5.3. Нонсенс-мутации в генах SUP45 и SUP

5.5.3.1. Локализация нонсенс-мутаций

5.5.3.2. Нуклеотидное окружение нонсенс-мутаций

5.5.3.3. Плейотропные эффекты мутаций sup45-n nsup35-n

5.5.4. Увеличение количества тРНК у мутантов по генам

SUP45 и SUP

Глава 6. ИДЕНТИФИКАЦИЯ БЕЛКА РАВР, КАК

ВЗАИМОДЕЙСТВУЮЩЕГО С ФАКТОРОМ ТЕРМИНАЦИИ eRF

6.1. Белок РАВР и его роль в трансляции (обзор 213 литературы)

6.1.1. Семейство белков РАВР

6.1.2. Структура белка РАВРС

6.1.3. Ядерный белок PABPN

6.1.4. Участие РАВР в полиаденилировании

6.1.5. Роль РАВР в транспорте мРНК из ядра в цитоплазму

6.1.6. Функции белка РАВРС в трансляции

6.1.7. Участие РАВРС в деградации мРНК

6.2. Идентификация белков, взаимодействующих с 225 белком eRF3 человека

6.2.1. Скрининг библиотеки кДНК Н. sapiens. Выявление 225 белков РАВРС 1 и iPABP, как белков, взаимодействующих с eRF

6.2.2. Взаимодействие полноразмерных бежов РАВРС 1 и 227 eRF3 в двугибридной системе

6.2.3. Участок РАВРС 1, взаимодействующий с eRF3, 228 локализован в С-терминальном домене этого белка

6.3. еРАВР X. laevis - новый белок семейства РАВР

6.3.1. Скрининг библиотеки кДНКХ laevis. Выявление 230 белка еРАВР, как белка, взаимодействующего с eRF

6.3.2. Сравнение последовательности белка еРАВР с 231 другими белками семейства РАВР

6.3.3. Белки еРАВР и РАВР1X laevis связываются с белком 233 eRF3 in vitro

6.3.4. Белок еРАВР способен компенсировать дизрупцию 234 гена РАВ1 дрожжей S. cerevisiae

6.4. Взаимодействие белков Pabl и eRF3 в клетках 236 дрожжей

6.4.1. Взаимодействие дрожжевых бежов eRF3 и Pabl в 236 двугибридной системе

6.4.2. Идентификация минимальных взаимодействующих 238 доменов белков Pabl и eRF

6.4.3. Участки взаимодействия eRF3 с белками Pabl и Slal 240 различны

6.4.4. Антисупрессорный эффект Pabl в клетках дрожжей, 241 содержащих мутацию sup

6.4.6.

6.5.1.

6.5.2.

6.6. 6.6.1. 6.6.2.

6.6.3.

6.6.4.

Глава 7.

Сверхэкспрессия РАВ1 приводит к подавлению супрессии, вызванной присутствием фактора [Р57*] Увеличение содержания бежа РаЫ в клетке приводит 251 к снижению фенотипической супрессии, индуцированной паромомицином

Консервативность взаимодействия белков eRF3 и 252 РАВР в эволюции

Полноразмерные белки eRF3 и РАВР из разных видов способны взаимодействовать друг с другом

Выявление участков РАВР и eRF3, взаимодействующих друг с другом у разных видов

Роль белка РАВР в терминации трансляции обсуждение)

Консервативность участков РАВР, взаимодействующих с eRF3 у разных видов Консервативность участков eRF3, взаимодействующих 258 с РАВР у разных видов

Роль белка РаЫ в терминации трансляции у дрожжей 262 Эволюционная консервативность связи терминации 266 трансляции и деградации мРНК

ЭВОЛЮЦИОННАЯ КОНСЕРВАТИВНОСТЬ 268 СИСТЕМЫ ТЕРМИНАЦИИ ТРАНСЛЯЦИИ У ЭУКАРИОТ (Заключение)

ВЫВОДЫ

Введение диссертации (часть автореферата) на тему «Генетический контроль терминации трансляции у эукариот»

МАТЕРИАЛЫ И МЕТОДЫ 17 В работе использовали стандартные однобуквенные или трехбуквенныеобозначения аминокислот.

Заключение диссертации по теме «Генетика», Журавлева, Галина Анатольевна

Выводы

1. Клонирование гомолога гена SUP35 S. cerevisiae из X. laevis позволило идентифицировать один из двух эукариотических факторов терминации - eRF3. Белки eRF3 и eRFl взаимодействуют друг с другом.

2. Гомологи eRF3 из Н. sapiens, М. musculus и X. laevis, лишенные своих N-терминальных доменов, способны функционировать в клетках дрожжей. Белок mGSPT2 (eRF3b) М. musculus способен замещать in vivo дрожжевой белок Sup35/eRF3, в отличие от его гомолога из того же организма mGSPTl (eRF3a).

3. Гены HBS1 S. cerevisiae и eRFS Н. sapiens, не могут компенсировать делецию гена SUPS5 S. cerevisiae. Белок Hbsl не взаимодействует с белками eRFl и eRF3. Таким образом, белки семейства eRFS не способны осуществлять функции eRF3.

4. В качестве белков, взаимодействующих с eRF3, выявлены РАВРС1 и iPABP, принадлежащие к семейству белков, связывающихся с поли(А)-концами мРНК. Обнаружен новый белок семейства РАВР - еРАВР XJaevis. Белок еРАВР взаимодействует с eRF3 in vivo и in vitro. Белок еРАВР способен компенсировать делецию гена РАВ1 дрожжей S. cerevisiae.

5. Во взаимодействии фактора терминации eRF3 с белком РАВР принимают участие N-терминальный домен eRF3 и С-терминальный домен РАВР.

6. Впервые показано, что белок Pabl S. cerevisiae способен влиять на процесс терминации трансляции за счет взаимодействия с eRF3.

7. Показано, что значительную долю омнипотентных супрессорных мутаций в генах SUP45 и SUP35 составляют нонсенс-мутации, приводящие к уменьшению содержания белков eRFl и eRF3.

8. Большинство миссенс-мутаций в гене SUP45 приводят к заменам аминокислот в N-терминальном домене бежа eRFl, не вызывая уменьшения количества белка eRFl и нарушения его взаимодействия с белком eRF3. Проанализированные миссенс-мутации в гене SUP35 приводят к заменам аминокислот в С-терминальном домене белка eRF3, не вызывая уменьшения количества белка eRF3 и нарушения его взаимодействия с белком eRFl.

9. Штаммы, содержащие мутации в генах SUP45 и SUP35, характеризуются повышенным содержанием различных типов тРНК. Жизнеспособность нонсенс-мутантов по жизненно-важным генам SUP45 и SUP35 может быть связана с увеличением содержания тРНК в мутантных клетках.

10. Белки eRFl и eRF3, а также eRF3 и РАВР из разных видов способны взаимодействовать друг с другом, что свидетельствует о консервативности белковых комплексов, участвующих в терминации трансляции у различных эукариотических организмов.

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