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Heat shock protein (hsp90) interacts with smooth muscle calponin and affects calponin-binding to actinстатья
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: 18 июля 2013 г.
- Авторы: Ma Y.S., Bogatcheva N.V., Gusev N.B.
- Журнал: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
- Том: 1476
- Номер: 2
- Год издания: 2000
- Первая страница: 300
- Последняя страница: 310
- DOI: 10.1016/S0167-4838(99)00250-2
- Аннотация: Interaction of smooth muscle calponin with 90 kDa heat shock protein (hsp90) was analyzed by means of native gel electrophoresis and affinity chromatography. Under conditions used, calponin and hsp90 form a complex with an apparent dissociation constant in the micromolar range. The major hsp90-binding site is located in the N-terminal (residues 7-144) part of calponin. Addition of calponin to actin-tropomyosin complex results in formation of actin bundles. Hsp90 partially prevents bundle formation without affecting the molar ratio calponin/actin in single actin filaments or actin bundles. At low ionic strength, calponin induces polymerization of G-actin. Hsp90 decreases calponin-induced polymerization of G-actin. It is supposed that hsp90 may be involved in the assembly of actin filaments. (C) 2000 Elsevier Science B.V. All rights reserved.
- Добавил в систему: Гусев Николай Борисович