FEBS Letters | |
Conformational changes in subdomain‐2 of G‐actin upon polymerization into F‐actin and upon binding myosin subfragment‐1 | |
Fievez, Stéphane1  Carlier, Marie-France1  | |
[1] Laboratoire d'Enzymologie, CNRS, 91198 Gif-sur-Yvette, France | |
关键词: Actin; Myosin; Actomysin interaction; Conformational change; Limited proteolysis; | |
DOI : 10.1016/0014-5793(93)81212-I | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 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, α-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-S1 complexes, and provide information on the mechanism of S1-induced polymerization of G-actin.
【 授权许可】
Unknown
【 预 览 】
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