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Effect of disulfide crosslinking on thermal transitions and chaperone-like activity of human small heat shock protein HspB1статья
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: 20 сентября 2015 г.
- Авторы: Chalova Anna S., Sudnitsyna Maria V., Semenyuk Pavel I., Orlov Victor N., Gusev Nikolai B.
- Журнал: Cell Stress and Chaperones
- Том: 19
- Номер: 6
- Год издания: 2014
- Издательство: Cell Stress Society International
- Местоположение издательства: United States
- Первая страница: 963
- Последняя страница: 972
- DOI: 10.1007/s12192-014-0520-9
- Аннотация: Temperature-induced conformational changes of reduced and oxidized HspB1 crosslinked by disulfide bond between single Cys137 of neighboring monomers were analyzed by means of different techniques. Heating of reduced HspB1 was accompanied by irreversible changes of Trp fluorescence, whereas oxidized HspB1 underwent completely reversible changes of fluorescence. Increase of the temperature in the range of 20-70 °C was accompanied by self-association of both reduced and oxidized protein. Further increase of the temperature led to formation of heterogeneous mixture of large self-associated complexes of reduced HspB1 and to formation of smaller and less heterogeneous complexes of oxidized HspB1. Heat-induced changes of oligomeric state of reduced HspB1 were only partially reversible, whereas the corresponding changes of oligomeric state of oxidized HspB1 were almost completely reversible. Oxidation resulted in decrease of chaperone-like activity of HspB1. It is concluded that oxidative stress, inducing formation of disulfide bond, can affect stability and conformational mobility of human HspB1.
- Добавил в систему: Гусев Николай Борисович