Новый механизм Ca2+-зависимой регуляции родопсинкиназы
В то время как активность протеинкиназ ОЫК1 и ОЛК7 регулируется Са /рековерином, активность других незрительных протеинкиназ из семейства ОЛК регулируется Са /кальмодулином. При этом к моменту начала настоящей работы в литературе имелись сведения о том, что кальмодулин споо асобен Сазависимым образом связываться с родопсинкиназой. Однако информация о влиянии кальмодулина на функциональную… Читать ещё >
Содержание
- Список сокращений
1. Обзор литературы: «Родопсинкиназа как представитель семейства протеинкиназ рецепторов, сопряжённых с О-белками».
1.1. Рецепторы, сопряжённые с О-белками, и их протеинкиназы.
1.1.1. Рецепторы, сопряжённые с О-белками.
1.1.2. Десенситизация рецепторов, сопряжённых с О-белками.
1.1.3. Семейство протеинкиназ рецепторов, сопряжённых с О-белками.
1.2. Экспрессия вИК в различных клетках и тканях.
1.3. Структурная организация протеинкиназ рецепторов, сопряжённых с О-белками.
1.4. Устройство генов, кодирующих протеинкиназы О-белок-сопряжённых рецепторов.
1.5. Внутриклеточная локализация протеинкиназ О-белок-сопряжённых рецепторов.
1.6. Механизм активации протеинкиназ рецепторов, сопряжённых с О-белками, активированными рецепторами.
1.7. Регуляция активности протеинкиназ рецепторов, сопряжённых с О-белками.
1.7.1. Аутофосфорилирование и фосфорилирование под действием других протеинкиназ.
1.7.2. Са2±зависимая регуляция.
1.7.3. Другие механизмы регуляции активности ОМС.
1.8. Родопсинкиназа и фосфорилирование родопсина.
1.8.1. Общая схема фототрансдукции.
1.8.2. Взаимодействие родопсинкиназы с родопсином и его фосфорилирование.
1.8.3. Участки фосфорилирования родопсина родопсинкиназой.
1.8.4. Рековерин как Са -сенсор родопсинкиназы.
2. Материалы и методы.
2.1. Использованные материалы и бактериальные штаммы.
2.2. Приготовление Са -буферных растворов.
2.3. Выделение наружных сегментов палочек сетчатки.
2.4. Получение фоторецепторных мембран, отмытых мочевиной или гипотоническим буфером.
2.5. Очистка родопсинкиназы из наружных сегментов палочек.
2.6. Очистка кальмодулина из мозга быка.
2.7. Приготовление химически компетентных бактериальных клеток
2.8. Трансформация бактериальных клеток плазмидной ДНК.
2.9. Выделение плазмидной ДНК.
2.10. Экспрессия в бактериальных клетках и очистка рекомбинантного рековерина.
2.11. Определение активности родопсинкиназы.
2.12. Получение рекомбинатных фрагментов родопсинкиназы.
2.12.1. Конструирование генов, кодирующих фрагменты родопсинкиназы в виде химерных белков с глутатион 8-трансферазой.
2.12.2. Отбор клонов.
2.12.3. Экспрессия в бактериальных клетках и очистка химерных белков 08Т-МС.
2.13. Спектроскопия поверхностного плазмонного резонанса.
2.13.1. Иммобилизация рекомбинантных фрагментов родопсинкиназы на поверхности сенсорного чипа.
2.13.2. Изучение взаимодействия фрагметов родопсинкиназы с кальмодулином и родопсином.
2.13.3. Определение констант диссоциации комплексов кальмодулина с фрагментами родопсинкиназы.
2.14. Метод аффинного соосаждения.
2.15. Аналитические процедуры.
2.15.1. Электрофорез ДНК в агарозном геле.
2.15.2. Электрофорез белков в полиакриламидном геле в присутствии додецилсульфата натрия.
2.15.3. Иммуноблоттинг.
2.15.4. Измерение концентрации белков.
3. Результаты и обсуждение.
3.1. Са2±зависимая регуляция родопсинкиназы кальмодулином.
3.1.1. Изучение влияния кальмодулина на фосфорилирование родопсина.
3.1.2. Выявление участков связывания кальмодулина в молекуле родопсинкиназы.
3.1.2.1. Изучение взаимодействия 1Г- и С-концевого регуляторных доменов родопсинкиназы с кальмодулином.
3.1.2.2. Изучение взаимодействия фрагментов ]Ч-концевого домена родопсинкиназы с кальмодулином.
3.1.2.3. Изучение взаимодействия кальмодулина с рековерин-связывающим участком родопсинкиназы.
3.2. Са2±зависимая регуляция родопсинкиназы рековерином и кальмодулином.
3.2.1. Изучение Са2±зависимой регуляции фосфорилирования родопсина в присутствии кальмодулина и рековерина.
3.2.2. Теоретическая модель механизма последовательного связывания рековерина и кальмодулина с родопсинкиназой.
3.3. Изучение роли кальмодулин-связывающего участка в функционировании родопсинкиназы.
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