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Myopathy-causing Q147P TPM2 mutation shifts tropomyosin strands further towards the open position and increases the proportion of strong-binding cross-bridges during the ATPase cycleстатья
Информация о цитировании статьи получена из
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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 Olga E., Simonyan Armen O., Kuleva Nadezhda V., Redwood Charles S., Borovikov Yurii S.
- Журнал: Biochimica et Biophysica Acta - Proteins and Proteomics
- Том: 1864
- Номер: 3
- Год издания: 2016
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 260
- Последняя страница: 267
- DOI: 10.1016/j.bbapap.2015.12.004
- Аннотация: The molecular mechanisms of skeletal muscle dysfunction in congenital myopathies remain unclear. The present study examines the effect of a myopathy-causing mutation Q147P in β-tropomyosin on the position of tropomyosin on troponin-free filaments and on the actin–myosin interaction at different stages of the ATP hydrolysis cycle using the technique of polarized fluorimetry. Wild-type and Q147P recombinant tropomyosins, actin, and myosin subfragment-1 were modified by 5-IAF, 1,5-IAEDANS or FITC-phalloidin, and 1,5-IAEDANS, respectively, and incorporated into single ghost muscle fibers, containing predominantly actin filaments which were free of troponin and tropomyosin. Despite its reduced affinity for actin in co-sedimentation assay, the Q147P mutant incorporates into the muscle fiber. However, compared to wild-type tropomyosin, it locates closer to the center of the actin filament. The mutant tropomyosin increases the proportion of the strong-binding myosin heads and disrupts the co-operation of actin and myosin heads during the ATPase cycle. These changes are likely to underlie the contractile abnormalities caused by this mutation.
- Добавил в систему: Карпичева Ольга Евгеньевна