SYNTHETIC PEPTIDE OF THE SEQUENCE-632-642 ON MYOSIN SUBFRAGMENT-1 INHIBITS ACTOMYOSIN ATPASE ACTIVITY

被引:18
作者
CHEUNG, P [1 ]
REISLER, E [1 ]
机构
[1] UNIV CALIF LOS ANGELES,INST MOLEC BIOL,LOS ANGELES,CA 90024
关键词
D O I
10.1016/0006-291X(92)92323-P
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
A synthetic peptide corresponding to a sequence 632-642 (S632-642) on the myosin subfragment 1 (S-1) heavy chain and spanning the 50 20 kDa junction of S-1 binds to actin in the presence and absence of S-1. The binding of 1.0 mole of peptide per actin causes almost complete inhibition of actomyosin ATPase activity and only partial inhibition of S-1 binding to actin. The binding of S632-642 to the N-terminal segment of actin is supported by competitive carbodiimide cross-linking of S-1 and S632-642 to actin and the catalytic properties of cross-linked acto-S-1 and actin-peptide complexes. These results show that the sequence 632-642 on S-1 is an autonomous binding site for actin and confirm the catalytic importance of its interactions with the N-terminal segment of actin. © 1992.
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页码:1143 / 1149
页数:7
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