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pubmed-article:1533157pubmed:abstractTextThe role of the N-terminal region of myosin light chain 1 (LC1) in actomyosin interaction was investigated using an IgG monoclonal antibody (2H2) directed against the N-terminal region of LC1. We defined the binding site of 2H2 by examining its cross-reactivity with myosin light chains from a variety of species and with synthetic oligopeptides. Our findings suggest that 2H2 is directed against the N-terminal region of LC1 which includes the trimethylated alanine residue at the N-terminus. In the presence of 2H2, the rate of actomyosin superprecipitation was reduced, although the extent was not. 2H2 caused a reduction in the Vmax of both myosin and chymotryptic S1(A1) actin-activated ATPase activity, while the Km appeared to be unaltered. The Mg(2+)-ATPase activity of myosin alone was also unaffected. Binding studies revealed that 2H2 did not prevent the formation of acto-S1 complex, either in the presence or in the absence of ATP, nor did it affect the ability of ATP to dissociate S1 from F-actin. Our findings suggest that the N-terminal region of LC1 is not essential for actin binding but is involved in modulating actin-activated ATPase activity of myosin.lld:pubmed
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pubmed-article:1533157pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:1533157pubmed:articleTitleUncoupling of actin-activated myosin ATPase activity from actin binding by a monoclonal antibody directed against the N-terminus of myosin light chain 1.lld:pubmed
pubmed-article:1533157pubmed:affiliationDepartment of Anatomy, University of Sydney, NSW, Australia.lld:pubmed
pubmed-article:1533157pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1533157pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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