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Glycyl-tRNA synthetase specifically binds to the poliovirus IRES to activate translation initiationстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 31 октября 2012 г.
- Авторы: Andreev D.E., Hirnet J., Terenin I.M., Dmitriev S.E., Niepmann M., Shatsky I.N.
- Журнал: Nucleic Acids Research
- Том: 28
- Год издания: 2012
- Издательство: Oxford University Press
- Местоположение издательства: United Kingdom
- DOI: 10.1093/nar/gks182
- Аннотация: Adaptation to the host cell environment to efficiently take-over the host cell's machinery is crucial in particular for small RNA viruses like picornaviruses that come with only small RNA genomes and replicate exclusively in the cytosol. Their Internal Ribosome Entry Site (IRES) elements are specific RNA structures that facilitate the 5' end-independent internal initiation of translation both under normal conditions and when the cap-dependent host protein synthesis is shut-down in infected cells. A longstanding issue is which host factors play a major role in this internal initiation. Here, we show that the functionally most important domain V of the poliovirus IRES uses tRNA(Gly) anticodon stem-loop mimicry to recruit glycyl-tRNA synthetase (GARS) to the apical part of domain V, adjacent to the binding site of the key initiation factor eIF4G. The binding of GARS promotes the accommodation of the initiation region of the IRES in the mRNA binding site of the ribosome, thereby greatly enhancing the activity of the IRES at the step of the 48S initiation complex formation. Moonlighting functions of GARS that may be additionally needed for other events of the virus-host cell interaction are discussed.
- Добавил в систему: Дмитриев Сергей Евгеньевич