Mechanism of the active movement of actin: Is actin sliding directly or indirectly related to binding with myosin and activation of myosin ATPase?

Ewa Prochniewicz, Toshio Yanagida

Research output: Contribution to journalArticlepeer-review

2 Scopus citations

Abstract

In the present work we examined the effect of crosslinking of polymerized and monomeric actin with glutaraldehyde, EDC and DSS on: 1) binding of actin to HMM in solution; 2) activation of HMM ATPase; 3) sliding movement of actin on glass-attached myosin; 4) properties of actin itself, like polymerizability and exchangeability of tightly bound nucleotide. The obtained data show that inhibition of sliding cannot be explained only by changes in the extent of activation of HMM ATPase and binding of actin to HMM; this result emphasizes the role of structural properties of actin in the mechanism of movement generation.

Original languageEnglish (US)
Pages (from-to)207-211
Number of pages5
JournalAdvances in Biophysics
Volume27
Issue numberC
DOIs
StatePublished - 1991

Fingerprint Dive into the research topics of 'Mechanism of the active movement of actin: Is actin sliding directly or indirectly related to binding with myosin and activation of myosin ATPase?'. Together they form a unique fingerprint.

Cite this