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Updated: Aug 19, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin
Published on: July 30, 2014
A novel 27/16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser234
A Vahdat1, C Miller, M Phillips
1Department of Chemistry and Biochemistry, University of California, Los Angeles 90095, USA.
Abstract:
A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleavage between Ser234 and Ser235 of F(MgADP)-actin complexed with BeFx. 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 degrees C by this cleavage. The in vitro motility and Vmax, but not Km, 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.
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