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The E117K mutation in beta-tropomyosin disturbs concerted conformational changes of actomyosin in muscle fibersстатья
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: 1 апреля 2017 г.
- Авторы: Karpicheva O.E., Redwood C.S., Borovikov Yu S.
- Журнал: Archives of Biochemistry and Biophysics
- Том: 549
- Год издания: 2014
- Издательство: Academic Press
- Местоположение издательства: United States
- Первая страница: 12
- Последняя страница: 16
- DOI: 10.1016/j.abb.2014.03.007
- Аннотация: The effect of the skeletal myopathy-causing E117K mutation in human β-tropomyosin on actomyosin structure during the ATPase cycle was studied using fluorescent probes bound to actin subdomain 1 and the myosin head. Multistep changes in flexural rigidity of actin filament and in spatial arrangement of actin subdomain 1 and myosin SH1 helix in troponin-free ghost muscle fibers were revealed. During the ATPase cycle E117K tropomyosin inhibited the rotation of subdomain 1 by 46% and the tilt of the SH1 helix by 49% compared with wild-type. At strong-binding stages the proportion of strong binding sub-states in the actomyosin population is decreased by the mutation. At weak-binding stages abnormally high numbers of switched-on actin monomers were observed, thus indicating a disturbance in concerted conformational changes of actomyosin. These structural alterations are likely to underlie the contractile deficit observed with this mutation.