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Calponin-like protein from mussel smooth muscle is a competitive inhibitor of actomyosin ATPase

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Abstract

The goal of this work was to elucidate the mechanism of inhibition of the actin-activated ATPase of myosin subfragment-1 (S1) by the calponin-like protein from mussel bivalve muscle. The calponin-like protein (Cap) is a 40-kDa actin-binding protein from the bivalve muscle of the mussel Crenomytilus grayanus. Kinetic parameters V max and K ATPase of actomyosin ATPase in the absence and the presence of Cap were determined to investigate the mechanism of inhibition. It was found that Cap mainly causes increase in K ATPase value and to a lesser extent the decrease in V max, which indicates that it is most likely a competitive inhibitor of actomyosin ATPase. Analysis of V max and K ATPase parameters in the presence of tropomyosin revealed that the latter is a noncompetitive inhibitor of the actomyosin ATPase.

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Abbreviations

acto-S1:

complex of actin with myosin subfragment 1

AM:

actomyosin

Cap:

calponin-like protein

DTT:

dithiothreitol

h1:

smooth muscle calponin of vertebrates

K ATPase :

apparent K m for actin

K m :

Michaelis constant

S1:

myosin subfragment 1

Tm:

tropomyosin

V max :

maximal rate of ATPase

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Authors and Affiliations

  1. Institute of Cytology, Russian Academy of Sciences, 194064, St. Petersburg, Russia

    V. V. Sirenko & Y. S. Borovikov

  2. Zhirmunsky Institute of Marine Biology, Far Eastern Division, Russian Academy of Sciences, 690041, Vladivostok, Russia

    A. V. Dobrzhanskaya & N. S. Shelud’ko

Authors
  1. V. V. Sirenko
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  2. A. V. Dobrzhanskaya
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  3. N. S. Shelud’ko
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  4. Y. S. Borovikov
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Corresponding authors

Correspondence to N. S. Shelud’ko or Y. S. Borovikov.

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Original Russian Text © V. V. Sirenko, A. V. Dobrzhanskaya, N. S. Shelud'ko, Y. S. Borovikov, 2016, published in Biokhimiya, 2016, Vol. 81, No. 1, pp. 85-91.

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Sirenko, V.V., Dobrzhanskaya, A.V., Shelud’ko, N.S. et al. Calponin-like protein from mussel smooth muscle is a competitive inhibitor of actomyosin ATPase. Biochemistry Moscow 81, 28–33 (2016). https://doi.org/10.1134/S000629791601003X

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  • DOI: https://doi.org/10.1134/S000629791601003X

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