Geeves, Michael A. and Griffiths, Hugh and Mijailovich, Srboljub M. and Smith, David (2011) Cooperative [Ca²+]-dependent regulation of the rate of myosin binding to actin: solution data and the tropomyosin chain model. Biophysical Journal, 100 (11). pp. 2679-2687. ISSN 0006-3495. (doi:https://doi.org/10.1016/j.bpj.2011.04.020) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
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The regulation of muscle contraction by calcium involves interactions among actin filaments, myosin-S1, tropomyosin (Tm), and troponin (Tn). We have extended our previous model in which the TmTn regulatory units are treated as a continuous flexible chain, and applied it to transient kinetic data. We have measured the time course of myosin-S1 binding to actin-Tm-Tn filaments in solution at various calcium levels with [actin]/[myosin] ratios of 10 and 0.1, which exhibit modest slowing as [Ca(2+)] is reduced and a lag phase at low calcium. These observations can be explained if myosin binds to actin in two steps, where the first step is rate-limiting and blocked by TmTnI at low calcium, and the second step is fast, reversible, and controlled by the neighboring configuration of coupled tropomyosin-troponin units. The model can describe the calcium dependence of the observed myosin binding reactions and predicts cooperative calcium binding to TnC with competition between actin and Ca-TnC for the binding of TnI. Implications for theories of thin-filament regulation in muscle are discussed.
|Divisions:||Faculties > Sciences > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||03 Nov 2011 12:30 UTC|
|Last Modified:||15 Jul 2014 10:52 UTC|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/28347 (The current URI for this page, for reference purposes)|