Myosin II from rabbit skeletal muscle and Dictyostelium discoideum and its interaction with F‐actin studied by 1H NMR spectroscopy

FEBS Letters

Kany, Harry¹  Kalbitzer, Hans Robert¹  Wolf, Jones¹ 

[1] University of Regensburg, Institute of Biophysics and Physical Biochemistry, Lehrstuhl Biologie III, Universitätsstr. 31, 93040 Regensburg, Germany

关键词: Nuclear magnetic resonance;    Actin;    Myosin;   

DOI  :  10.1016/S0014-5793(02)02855-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Mg-F-actin occurs in two conformational states, I and M, where the N-terminal amino acids are either immobile or highly mobile. In the rigor or ADP complex of rabbit myosin S1 with Mg-F-actin the N-terminal acetyl group of actin stays in its highly mobile state. The same is true for the complexes with the myosin motor domain from Dictyostelium discoideum. This excludes a direct strong interaction of the N-terminal amino acids with myosin in the rigor state as suggested. An interaction of the N-terminus of F-actin with myosin is also not promoted by occupying its low-affinity binding site(s) with divalent ions. The N-terminal high-mobility region may be part of a structural system which has evolved for releasing inadequate stress applied to the actin filaments

【 授权许可】

Unknown