Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca2+-sensitivity of Actin-Myosin Interaction

We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility assay at high Са(2+) concentrations and the Са(2+)-sensitivity of the actin-myosin inter...

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Detalles Bibliográficos
Autores principales: Shchepkin, D.V., Matyushenko, A. M., Kopylova, G. V., Artemova, N. V., Bershitsky, S. Y., Tsaturyan, A. K., Levitsky, D. I.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: A.I. Gordeyev 2013
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3848074/
https://www.ncbi.nlm.nih.gov/pubmed/24303208
Descripción
Sumario:We show that the mutations D137L and G126R, which stabilize the central part of the tropomyosin (Tm) molecule, increase both the maximal sliding velocity of the regulated actin filaments in the in vitro motility assay at high Са(2+) concentrations and the Са(2+)-sensitivity of the actin-myosin interaction underlying this sliding. Based on an analysis of the recently published data on the structure of the actin–Tm–myosin complex, we suppose that the physiological effects of these mutations in Tm can be accounted for by their influence on the interactions between the central part of Tm and certain sites of the myosin head.

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