Selective perturbation of the myosin recovery stroke by point mutations at the base of the lever arm affects ATP hydrolysis and phosphate release

András Málnási-Csizmadia, Judit Tóth, David S. Pearson, Csaba Hetényi, László Nyitray, Michael A. Geeves, Clive R. Bagshaw, Mihály Kovács

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

After ATP binding the myosin head undergoes a large structural rearrangement called the recovery stroke. This transition brings catalytic residues into place to enable ATP hydrolysis, and at the same time it causes a swing of the myosin lever arm into a primed state, which is a prerequisite for the power stroke. By introducing point mutations into a subdomain interface at the base of the myosin lever arm at positions Lys84 and Arg 704, we caused modulatory changes in the equilibrium constant of the recovery stroke, which we could accurately resolve using the fluorescence signal of single tryptophan Dictyostelium myosin II constructs. Our results shed light on a novel role of the recovery stroke: fine-tuning of this reversible equilibrium influences the functional properties of myosin through controlling the effective rates of ATP hydrolysis and phosphate release.

Original languageEnglish
Pages (from-to)17658-17664
Number of pages7
JournalJournal of Biological Chemistry
Volume282
Issue number24
DOIs
Publication statusPublished - Jun 15 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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