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

D. V. Shchepkin; Щепкин Д. В.; A. M. Matyushenko; Матюшенко A. M.; G. V. Kopylova; Копылова Г. В.; N. V. Artemova; Артемова Н. В.; S. Y. Bershitsky; Бершицкий С. Ю.; A. K. Tsaturyan; Цатурян A. K.; D. I. Levitsky; Левицкий Д. И.

doi:10.32607/20758251-2013-5-3-126-129

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:
1. Institute of Immunology and Physiology
2. Bach Institute of Biochemistry, Russian Academy of Sciences
3. Institute of Mechanics, Lomonosov Moscow State University
4. Belozersky Institute of Physico-Chemical Biology
Issue: Vol 5, No 3 (2013)
Pages: 126-129
Section: Short communications
Submitted: 17.01.2020
Published: 15.09.2013
URL: https://actanaturae.ru/2075-8251/article/view/10597
DOI: https://doi.org/10.32607/20758251-2013-5-3-126-129
ID: 10597

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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.

Keywords

actin-myosin interaction, in vitro motility assay, regulation of muscle contraction, tropomyosin

References

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

Full Text

Abstract

Keywords

About the authors

D. V. Shchepkin

A. M. Matyushenko

G. V. Kopylova

N. V. Artemova

S. Y. Bershitsky

A. K. Tsaturyan

D. I. Levitsky

References

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