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Polyadenylate-binding protein-interacting proteins PAIP1 and PAIP2 affect translation terminationстатья 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: 15 сентября 2020 г.
- Авторы: Ivanov Alexander, Shuvalova Ekaterina, Egorova Tatiana, Shuvalov Alexey, Sokolova Elizaveta, Bizyaev Nikita, Shatsky Ivan, Terenin Ilya, Alkalaeva Elena
- Журнал: Journal of Biological Chemistry
- Том: 294
- Номер: 21
- Год издания: 2019
- Издательство: American Society for Biochemistry and Molecular Biology Inc.
- Местоположение издательства: United States
- Первая страница: 8630
- Последняя страница: 8639
- DOI: 10.1074/jbc.ra118.006856
- Аннотация: Polyadenylate-binding protein (PABP) stimulates translation termination via interaction of its C-terminal domain with eukaryotic polypeptide chain release factor, eRF3. Additionally, two other proteins, poly(A)-binding protein-interacting protein 1 and 2 (PAIP1 and PAIP2), bind the same domain of PABP and regulate its translation-related activity. To study the biochemistry of eRF3 and PAIP1/2 competition for PABP binding, we quantified the effects of PAIPs on translation termination in the presence or absence of PABP. Our results demonstrated that both PAIP1 and PAIP2 prevented translation termination at premature termination codon (PTC), by controlling PABP activity. Moreover, PAIP1 and PAIP2 inhibited the activity of free PABP on translation termination in vitro. However, after binding the poly(A) tail, PABP became insensitive to suppression by PAIPs and efficiently activated translation termination in the presence of eRF3a. Additionally, we revealed that PAIP1 binds eRF3 in solution, which stabilizes the post-termination complex (postTC). These results indicated that PAIP1 and PAIP2 participate in translation termination and are important regulators of readthrough at PTC.
- Добавил в систему: Теренин Илья Михайлович