The rôle of the proline‐rich region in A1‐type myosin essential light chains: implications for information transmission in the actomyosin complex

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Abstract
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.