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60S dynamic state of bacterial ribosome is fixed by yeast mitochondrial initiation factor 3статья Исследовательская статья
Информация о цитировании статьи получена из
Web of Science,
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 24 октября 2018 г.
- Авторы: Sergey Levitskii, Ksenia Derbikova, Baleva Maria V., Anton Kuzmenko, Golovin Andrey V., Ivan Chicherin, Krasheninnikov Igor A., Piotr Kamenski
- Журнал: PeerJ
- Том: 6
- Год издания: 2018
- Издательство: PeerJ
- Местоположение издательства: San Francisco
- Первая страница: 5620
- DOI: 10.7717/peerj.5620
- Аннотация: The processes of association and dissociation of ribosomal subunits are of great importance for the protein biosynthesis. The mechanistic details of these processes, however, are not well known. In bacteria, upon translation termination, ribosome dissociates into subunits which is necessary for its further involvement into new initiation step. The dissociated state of ribosome is maintained by initiation factor 3 (IF3) which binds to free small subunits and prevents their premature association with the large subunits. In this work, we have exchanged IF3 in Escherichia coli cells by its ortholog from Saccharomyces cerevisiae mitochondria (Aim23p) and showed that yeast protein cannot functionally substitute the bacterial one and is even slightly toxic for bacterial cells. Our in vitro experiments have demonstrated that Aim23p does not split E. coli ribosomes into subunits. Instead, it fixes a state of ribosomes characterized by sedimentation coefficient about 60S which is not a stable structure but rather reflects a shift of dynamic equilibrium between associated and dissociated states of the ribosome. Mitochondria-specific terminal extensions of Aim23p are necessary for “60S state” formation, and molecular modeling results point out that these extensions might stabilize the position of the protein on the bacterial ribosome.
- Добавил в систему: Каменский Петр Андреевич