A myosin II mutation uncouples ATPase activity from motility and shortens step size

Coleen T. Murphy, R. S. Rock, J. A. Spudich

Research output: Contribution to journalArticle

66 Scopus citations

Abstract

It is thought that Switch II of myosin, kinesin and G proteins has an important function in relating nucleotide state to protein conformation. Here we examine a myosin mutant containing an S456L substitution in the Switch II region. In this protein, mechanical activity is uncoupled from the chemical energy of ATP hydrolysis so that its gliding velocity on actin filaments is only one-tenth of that of the wild type. The mutant spends longer in the strongly bound state and exhibits a shorter step size, which together account for the reduction in in vitro velocity. This is the first single point mutation in myosin that has been found to affect step size.

Original languageEnglish (US)
Pages (from-to)311-315
Number of pages5
JournalNature Cell Biology
Volume3
Issue number3
DOIs
StatePublished - Mar 20 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology

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