Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility

Ewa Prochniewicz, Toshio Yanagida

Research output: Contribution to journalArticlepeer-review

85 Scopus citations

Abstract

The effects of crosslinking of monomeric and polymeric actin with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC), disuccinimidyl suberate (DSS) and glutaraldehyde on the interaction with heavy meromyosin (HMM) in solution and on the sliding movement on glass-attached HMM were examined. The vmax values of actin-activated HMM ATPase decreased in the following order: intact actin = EDC F-actin > DSS actin > glutaraldehyde F-actin = glutaraldehyde G-actin > EDC G-actin. The affinity of actin for HMM in the presence of ATP decreased in the following order: DSS actin > glutaraldehyde F-actin = glutaraldehyde G-actin > intact actin > EDC F-actin > EDC G-actin. However, sliding movement was inhibited only in the case of glutaraldehyde-crosslinked F and G-actin and EDC-crosslinked G-actin. Interestingly, after copolymerization of "non-motile" glutaraldehyde or EDC-crosslinked monomers with "motile" monomers of intact actin sliding of the copolymers was observed and its rate was independent of the type of crosslinked monomer, i.e. of the manner of their interaction with HMM. These data strongly indicate that inhibition of the sliding of actin by crosslinking cannot be explained entirely by changes in the vmax value or affinity for myosin heads. We conclude that movement is generated by interaction of myosin with segments of F-actin containing a number of intact monomers, and the mechanism of inhibition involves an effect of the crosslinkers on the structure of F-actin itself.

Original languageEnglish (US)
Pages (from-to)761-772
Number of pages12
JournalJournal of Molecular Biology
Volume216
Issue number3
DOIs
StatePublished - Dec 5 1990

Bibliographical note

Copyright:
Copyright 2014 Elsevier B.V., All rights reserved.

Fingerprint Dive into the research topics of 'Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility'. Together they form a unique fingerprint.

Cite this