The proline-rich region of A1-type myosin essential light chains plays a critical role in information transmission in the actomyosin complex by coupling actin binding to kinetic modulation.
Identifies a modulator of myosin kinetics in animal models; extends molecular insights but leaves open relevance to human cardiac function.
The proline-rich region of A1-type myosin essential light chains functions as a spacer arm separating an actin binding site at the extreme N-terminus from the remainder of the protein. Alteration of the length of this region leaving the actin binding site intact results in altered actin-activated MgATPase kinetics when these light chains are hybridised into myosin subfragment-1. In the case of a mutant in which the length of the proline-rich region was doubled, actin binding by the light chain was uncoupled from kinetic modulation. The implications of this result for information transmission in the actomyosin complex are discussed.
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Timson et al. (1997) studied this question.
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