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

FEBS Letters

Trayer, Ian P¹  Timson, David J¹ 

[1] School of Biochemistry, The University of Birmingham, PO Box 363, Edgbaston, Birmingham B15 2TT, UK

关键词: Muscle contraction;    Actin binding;    Proline;    Protein engineering;    ATPase;    Protein-protein interaction;    S1;    myosin subfragment-1;    S1A1;    S1A2;    S1 containing alkali 1 (A1) or alkali 2 (A2) essential light chain;    RLC;    myosin regulatory light chain;    ELC;    myosin essential light chain;    HmAtELC;    human atrial ELC;    HmAtELCΔXP;    HmAtELC lacking the proline-rich region;    HmAtELC2XP;    HmAtELC with a proline-rich region twice the length of the wild type;    EDC;    1-ethyl-3-[3-(dimethylamino)propyl] carbodiimide;    F-actin;    filamentous actin;    Xxx;    any amino acid;    TEA-HCl;    triethanolamine hydrochloride;    A 280;    1 mg/ml;    absorbance at 280 nm of a 1 mg ml−1 solution;   

DOI  :  10.1016/S0014-5793(96)01314-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown