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Enzymatic activity of the ribosome-bound nascent polypeptideстатья
Информация о цитировании статьи получена из
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Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 7 сентября 2016 г.
- Авторы: Makeyev E.V., Kolb V.A., Spirin A.S.
- Журнал: FEBS Letters
- Том: 378
- Номер: 2
- Год издания: 1996
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 166
- Последняя страница: 170
- Аннотация: Firefly luciferase was shown to be completely folded and thus enzymatically active immediately upon release from the ribosome [Kolb et al. (1994) EMBO J. 13, 3631-3637]. However, no luciferase activity was observed while full-length luciferase was attached to the ribosome as a peptidyl-tRNA, probably because the C-terminal portion of the enzyme is masked by the ribosome and/or ribosome-associated proteins. Here we have demonstrated that the ribosome-bound enzyme acquires the enzymatic activity when its C-terminus is extended by at least 26 additional amino acid residues. The results demonstrate that the acquisition of the final native conformation by a nascent protein does not need the release of the protein from the ribosome.
- Добавил в систему: Колб Вячеслав Адамович