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Truncation of vertebrate striated muscle myosin light chains disturbs calcium-induced structural transitions in synthetic myosin filamentsстатья
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: 3 февраля 2015 г.
- Авторы: Podlubnaya Z.A., Kakol I., Moczarska A., Stepkowski D., Udaltsov S.
- Журнал: Journal of Structural Biology
- Том: 131
- Номер: 3
- Год издания: 2000
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 225
- Последняя страница: 233
- DOI: 10.1006/jsbi.2000.4265
- Аннотация: Electron microscopy and negative staining techniques have been used to show that the proteolytic removal of 13 amino acids from the N-terminus of essential light chain 1 and 19 amino acids from the N-terminus of the regulatory light chain of rabbit skeletal and cardiac muscle myosins destroys Ca2+- induced reversible movement of subfragment-2 (S2) with heads (S1) away from the backbone of synthetic myosin filaments observed for control assemblies of the myosin under near physiological conditions. This is the direct demonstration of the contribution of the S2 movement to the Ca2+-sensitive structural behavior of rabbit cardiac and skeletal myosin filaments and of the necessity of intact light chains for this movement. In muscle, such a mobility might play an. important role in proper functioning of the myosin filaments. The impairment of the Ca2+-dependent structural behavior of S2 with S1 on the surface of the synthetic myosin filaments observed by us may be of direct relevance to some cardiomyopathies, which are accompanied by proteolytic breakdown or dissociation of myosin light chains. (C) 2000 Academic Press.
- Добавил в систему: Удальцов Сергей Николаевич