REGULATORY LIGHT CHAIN INFLUENCES ALTERATIONS OF MYOSIN HEAD INDUCED BY ACTIN

被引：13
作者：
BABIYCHUK, EB
STEPKOWSKI, D
DANILOVA, VM
KAKOL, I
机构：
[1] M NENCKI INST EXPTL BIOL, DEPT CELLULAR BIOCHEM, UL PASTEURA 3, PL-02093 WARSAW, POLAND
[2] TG SHEVCHENKO STATE UNIV, PHYSIOL RES INST, KIEV, UKRAINE, USSR
来源：
FEBS LETTERS | 1991年 / 295卷 / 1-3期
关键词：
SKELETAL MUSCLE MYOSIN; REGULATORY LIGHT CHAIN; ACTIN; LIMITED PROTEOLYSIS; MYOSIN PHOSPHORYLATION;
D O I：
10.1016/0014-5793(91)81383-J
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
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 meromyosin 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.
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收藏
页码：55 / 58
页数：4
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