Email this article Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca 2+-sensitivity of Actin-Myosin Interaction
- Authors: Shchepkin D.V.1, Matyushenko A.M.2, Kopylova G.V.1, Artemova N.V.2, Bershitsky S.Y.1, Tsaturyan A.K.3, Levitsky D.I.2,4
-
Affiliations:
- Institute of Immunology and Physiology
- Bach Institute of Biochemistry, Russian Academy of Sciences
- Institute of Mechanics, Lomonosov Moscow State University
- Belozersky Institute of Physico-Chemical Biology
- Issue: Vol 5, No 3 (2013)
- Pages: 126-129
- Section: Short communications
- URL: https://actanaturae.ru/2075-8251/article/view/10597
- DOI: https://doi.org/10.32607/20758251-2013-5-3-126-129
- ID: 10597
Cite item
Abstract
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.
About the authors
D. V. Shchepkin
Institute of Immunology and Physiology
Author for correspondence.
Email: levitsky@inbi.ras.ru
Russian Federation
A. M. Matyushenko
Bach Institute of Biochemistry, Russian Academy of Sciences
Email: levitsky@inbi.ras.ru
Russian Federation
G. V. Kopylova
Institute of Immunology and Physiology
Email: levitsky@inbi.ras.ru
Russian Federation
N. V. Artemova
Bach Institute of Biochemistry, Russian Academy of Sciences
Email: levitsky@inbi.ras.ru
Russian Federation
S. Y. Bershitsky
Institute of Immunology and Physiology
Email: levitsky@inbi.ras.ru
Russian Federation
A. K. Tsaturyan
Institute of Mechanics, Lomonosov Moscow State University
Email: levitsky@inbi.ras.ru
Russian Federation
D. I. Levitsky
Bach Institute of Biochemistry, Russian Academy of Sciences; Belozersky Institute of Physico-Chemical Biology
Email: levitsky@inbi.ras.ru
Russian Federation
References
- McKillop D.F.A., Geeves M.A. // Biophys. J. 1993, V.65, P.693-701
- Nevzorov I.A., Levitsky D.I. // Biochemistry (Moscow). 2077, V.76, №13, P.1507-1527
- Sumida J.P., Wu E., Lehrer S.S. // J. Biol. Chem. 2008, V.283, P.6728-6734
- Nevzorov I.A., Nikolaeva O.P., Kainov Y.A., Redwood C.S., Levitsky D.I. // J. Biol. Chem. 2011, V.286, P.15766-15772
- Shchepkin D.V., Kopylova G.V., Nikitina L.V., Katsnelson L.B., Bershitsky S.Y. // Biochem. Biophys. Res. Commun. 2010, V.401, №1, P.159-163
- Homsher E., Kim B., Bobkova A., Tobacman L.S. // Biophys. J. 1996, V.70, P.1881-1892
- Mashanov G.I., Molloy J.E. // Biophys. J. 2007, V.92, №6, P.2199-2211
- Behrmann E., Müller M., Penczek P.A., Mannherz H.G., Manstein D.J., Raunser S. // Cell. 2010, V.150, №2, P.327-338
- Lehman W., Craig R. // Adv. Exp. Med. Biol. 2008, V.644, P.95-109
Supplementary files
