Regulatory light chain influences alterations of myosin head induced by actin

FEBS Letters

Babiychuk, Eduard B.²  Danilova, Valentina M.²  Stepkowski, Dariusz¹  Kakol, Irena¹ 

[1] Department of Cellular Biochemistry, Nencki Institute of Experimental Biology, Warszawa, Poland;Research Institute of Physiology, Kiev State University, Kiev, U.S.S.R.

关键词: Skeletal muscle myosin;    Regulatory light chain;    Actin;    Limited proteolysis;    Myosin phosphorylation;   

DOI  :  10.1016/0014-5793(91)81383-J

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The effect of magnesium-for-calcium exchange and phosphorylation of regulatory light chain (LC₂) on structural organization of rabbit skeletal myosin head was studied by limited tryptic digestion. In the presence of actin, exchange of magnesium bound to LC₂ by calcium in dephosphorylated myosin accelerates the digestion of myosin and heavy meromysin heavy chain and increases the accumulation of a 50 kDa fragment. This effect is significantly diminished in the case of phosphorylated myosin. Thus, both phosphorylation and cation exchange influences the effect of actin binding on the structural organization of myosin head.

【 授权许可】

Unknown