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PubMed · 1731895

Electrostatic changes at the actomyosin-subfragment 1 interface during force-generating reactions.

S Highsmith·A J Murphy
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Abstract

The ionic strength dependence of the binding of rabbit skeletal muscle myosin subfragment 1, S1, to F-actin in the presence of saturating concentrations of MgATP or MgADP was analyzed in order to determine the association constants at zero ionic strength [K(0)] and the products of the net effective electric charges (magnitude of zMzA) at the binding interfaces. K(0) and magnitude of zM A were 1 x 10(6) M-1 and 17 esu2 for S1-MgADP,P, and 5 x 10(7) M-1 and 7 esu2 for S1-MgADP, respectively, for binding to F-actin at 25 degrees C. At ionic strengths near physiological, the increase in affinity is close to 10(4)-fold for this transition that may correspond to force generation in muscle fibers. The large, from 17 to 7 esu2, decrease in the electrostatic contribution to binding appears to be correlated with a much larger increase in nonelectrostatic interactions, unlike the simpler transition of actin-bound S1-MgADP to S1, which appears to be due entirely to electrostatic changes [Highsmith, S. (1990) Biochemistry 29, 10690-10694]. These results for acto-S1-MgADP,P to acto-S1-MgADP suggest that a substantial transformation of the actin binding site on S1 occurs even if there is a translocation to a new interface.

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ActinsActomyosinAdenosine DiphosphateAnimalsElectrochemistryKineticsMuscle ContractionMyosin SubfragmentsOsmolar ConcentrationProtein BindingRabbitsX-Ray DiffractionJournal ArticleResearch Support, U.S. Gov't, P.H.S.

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S Highsmith, A J Murphy. 1992-01-21. Electrostatic changes at the actomyosin-subfragment 1 interface during force-generating reactions.. https://doi.org/10.1021/bi00117a011

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