Stabilization of the Central Part of Tropomyosin Molecule Alters the Ca 2+-sensitivity of Actin-Myosin Interaction

Cover Page

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.


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

  1. McKillop D.F.A., Geeves M.A. // Biophys. J. 1993, V.65, P.693-701
  2. Nevzorov I.A., Levitsky D.I. // Biochemistry (Moscow). 2077, V.76, №13, P.1507-1527
  3. Sumida J.P., Wu E., Lehrer S.S. // J. Biol. Chem. 2008, V.283, P.6728-6734
  4. Nevzorov I.A., Nikolaeva O.P., Kainov Y.A., Redwood C.S., Levitsky D.I. // J. Biol. Chem. 2011, V.286, P.15766-15772
  5. 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
  6. Homsher E., Kim B., Bobkova A., Tobacman L.S. // Biophys. J. 1996, V.70, P.1881-1892
  7. Mashanov G.I., Molloy J.E. // Biophys. J. 2007, V.92, №6, P.2199-2211
  8. Behrmann E., Müller M., Penczek P.A., Mannherz H.G., Manstein D.J., Raunser S. // Cell. 2010, V.150, №2, P.327-338
  9. Lehman W., Craig R. // Adv. Exp. Med. Biol. 2008, V.644, P.95-109

Views

Abstract - 269

PDF (English) - 109

PDF (Russian) - 80

Cited-By


Article Metrics

Metrics Loading ...

Metrics powered by PLOS ALM

PlumX

Dimensions

Refbacks

  • There are currently no refbacks.

Copyright (c) 2013 Shchepkin D.V., Matyushenko A.M., Kopylova G.V., Artemova N.V., Bershitsky S.Y., Tsaturyan A.K., Levitsky D.I.

Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.

This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies