FEBS Letters | |
The effect of myosin light chain phosphorylation on the actin‐stimulated ATPase activity of myosin minifilaments | |
Levitsky, Dmitri I.2  Shuvalova, Lyudmila A.1  Poglazov, Boris F.1  | |
[1] A.N. Bach Institute of Biochemistry of the Academy of Sciences of the USSR, Moscow 117071, USSR;A. N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, Moscow 119899, USSR | |
关键词: Myosin; Phosphorylation; Actin-myosin interaction; ATP hydrolysis; (Rabbit skeletal muscle); LC2; myosin light chain 2; | |
DOI : 10.1016/0014-5793(87)80355-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
It has been shown that in the absence of KCl, the actin-stimulated Mg2+-ATPase activity of rabbit skeletal myosin minifilaments with phosphorylated regulatory lights chains (LC2) exceeds 3–4-fold that of myosin minifilaments with dephosphorylated LC2. Addition of KCl leads to a decrease in the difference between the two ATPase activities. LC2 phosphorylation considerably increases the rate of ATPase reaction and only slightly decreases the affinity of myosin minifilaments for F-actin. It is suggested that the unusual effect of LC2 phosphorylation on the kinetic parameters of the actin-stimulated ATPase reaction of myosin minifilaments can be accounted for by its influence on the interaction between myosin heads which results in the ordered self-assembly of minifilaments.
【 授权许可】
Unknown
【 预 览 】
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RO201912020289639ZK.pdf | 288KB | download |