A NOVEL 27 16 KDA FORM OF SUBTILISIN CLEAVED ACTIN - STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF CLEAVAGE BETWEEN SER(234) AND SER(235)/

Authors
VAHDAT A MILLER C PHILLIPS M MUHLRAD A REISLER E
Citation
A. Vahdat et al., A NOVEL 27 16 KDA FORM OF SUBTILISIN CLEAVED ACTIN - STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF CLEAVAGE BETWEEN SER(234) AND SER(235)/, FEBS letters, 365(2-3), 1995, pp. 149-151
Citations number
11
Categorie Soggetti
Biophysics,Biology
Journal title
FEBS letters → ACNP
ISSN journal
00145793
Volume
365
Issue
2-3
Year of publication
1995
Pages
149 - 151
Database
ISI
SICI code
0014-5793(1995)365:2-3<149:AN21KF>2.0.ZU;2-W
Abstract
A new 27/16 kDa form of cleaved actin was prepared by subtilisin cleav age between Ser(234) and Ser(235) of F(MgADP)-actin complexed with BeF x. The cleavage had little effect on actin-actin interactions as probe d in polymerization measurements and by electron microscopy, In circul ar dichroism melting experiments the thermostability of F-actin was re duced by about 10 degrees C by this cleavage, The in vitro motility an d 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 act in was unchanged by this modification.