CONFORMATIONAL-CHANGES IN SUBDOMAIN-2 OF G-ACTIN UPON POLYMERIZATION INTO F-ACTIN AND UPON BINDING MYOSIN SUBFRAGMENT-1

被引：24
作者：
FIEVEZ, S
CARLIER, MF
机构：
[1] Laboratoire d'Enzymologie, CNRS
来源：
FEBS LETTERS | 1993年 / 316卷 / 02期
关键词：
ACTIN; MYOSIN; ACTOMYOSIN INTERACTION; CONFORMATIONAL CHANGE; LIMITED PROTEOLYSIS;
D O I：
10.1016/0014-5793(93)81212-I
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 susceptibility of subdomain-2 of actin to different proteases has been examined, for G-actin, F-actin, G-actin-S1(A2) and F-actin-S1(A2) complexes on a comparative basis. The sites of subtilisin, alpha-chymotrypsin and trypsin attack, exposed on G-actin, are protected in F-actin, F-actin-S1(A2) as well as in the G-actin-S1(A2) complex. In contrast, a new cleavage site (Arg39-His40) for ArgC protease, which is protected in G-actin, is exposed in G-actin-S1(A2) as well as in F-actin and F-actin-S1(A2). These results are consistent with the previously proposed structural analogy between the ternary (G-actin)2S1 and the F-actin-S, complexes, and provide information on the mechanism of S1-induced polymerization of G-actin.
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页码：186 / 190
页数：5
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