A novelkDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser234 and Ser235

FEBS Letters

Reisler, Emil¹  Muhlrad, Andras²  Phillips, Martin¹  Miller, Carl¹  Vahdat, Arash¹ 

[1] Department of Chemistry and Biochemistry, and the Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA;Department of Oral Biology, Hadassah School of Dental Medicine, Hebrew University, Jerusalem 91010, Israel

关键词: Actin;    Proteolysis;    Actomyosin interaction;    Structure-function relationship;    S1;    myosin subfragment 1;   

DOI  :  10.1016/0014-5793(95)00446-G

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser²³⁴ and Ser²³⁵ of F(MgADP)-actin complexed with BeF_x. The cleavage had little effect on actin-actin interactions as probed in polymerization measurements and by electron microscopy. In circular dichroism melting experiments the thermostability of F-actin was reduced by about 10°C by this cleavage. The in vitro motility and V _max, but not K _m, of actomyosin ATPase were decreased by about 20% upon 27/16 kDa cleavage of F-actin. The binding of tropomyosin to actin was unchanged by this modification.

【 授权许可】

Unknown