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The product of uncl gene in F1F0-ATP synthase operon plays a chaperone-like role to assist c-ring assemblyстатья
Статья опубликована в высокорейтинговом журнале
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: 18 июля 2013 г.
- Авторы: Suzuki Toshiharu, Ozaki Yoko, Sone Nobuhito, Feniouk Boris A., Yoshida Masasuke
- Журнал: Proceedings of the National Academy of Sciences of the United States of America
- Том: 104
- Номер: 52
- Год издания: 2007
- Издательство: National Academy of Sciences
- Местоположение издательства: United States
- Первая страница: 20776
- Последняя страница: 20781
- DOI: 10.1073/pnas.0708075105
- Аннотация: Bacterial operons for F1F0-ATP synthase typically include an uncl gene that encodes a function-unknown small hydrophobic protein. When we expressed a hybrid F1F0 (F-1 from thermophilic Bacillus PS3 and Na+-translocating F-o from Propionigenium modestum) in Escherchia coli cells, we found that uncl derived from A modestum was indispensable to produce active enzyme; without uncl, c-subunits in F1Fo existed as monomers but not as functional c(11)-ring. When uncl was expressed from another plasmid at the same time, active F1Fo with c(11)-ring was produced. A plasmid containing only uncl and c-subunit gene produced c(11)-ring, but a plasmid containing only C-subunit gene did not. Direct interaction of Uncl protein with c-subunits was suggested from copurification of His-tagged Uncl protein and c-subunits, both in the state of c(11)-ring and c-monomers. Na+ induced dissociation of His-tagged Uncl protein from c(11)-ring but not from c-monomers. These results show that Uncl is a chaperone-like protein that assists c(11)-ring assembly from c-monomers in the membrane.
- Добавил в систему: Фенюк Борис Александрович