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The rôle of the proline‐rich region in A1‐type myosin essential light chains: implications for information transmission in the actomyosin complex
Author(s) -
Timson David J,
Trayer Ian P
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01314-2
Subject(s) - myosin , actin , immunoglobulin light chain , biophysics , myosin head , myosin light chain kinase , chemistry , proline , binding site , biochemistry , biology , amino acid , genetics , antibody
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.