A novel 27 16 kDa form of subtilisin cleaved actin: structural and functional consequences of cleavage between Ser234 and Ser235

Arash Vahdat, Carl Miller, Martin Phillips, Andras Muhlrad, Emil Reisler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

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°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.

Original languageEnglish
Pages (from-to)149-151
Number of pages3
JournalFEBS Letters
Volume365
Issue number2-3
DOIs
StatePublished - 29 May 1995

Keywords

  • Actin
  • Actomyosin interaction
  • Proteolysis
  • Structure-function relationship

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