Probes bound to myosin Cys-707 rotate during length transients in contraction

Thomas P. Burghardt, Susanna P. Garamszegi, Katalin Ajtai

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

It is widely conjectured that muscle shortens because portions of myosin molecules (the 'cross-bridges') impel the actin filament to which they transiently attach and that the impulses result from rotation of the cross- bridges. Crystallography indicates that a cross-bridge is articulated- consisting of a globular catalytic/actin-binding domain and a long lever arm that may rotate. Conveniently, a rhodamine probe with detectable attitude can be attached between the globular domain and the lever arm, enabling the observer to tell whether the anchoring region rotates. Well-established signature effects observed in shortening are tension changes resulting from the sudden release or quick stretch of active muscle fibers. In this investigation we found that closely correlated with such tension changes are changes in the attitude of the rhodamine probes. This correlation strongly supports the conjecture about how shortening is achieved.

Original languageEnglish (US)
Pages (from-to)9631-9636
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number18
DOIs
StatePublished - Sep 2 1997

Keywords

  • Energy transduction
  • Highly reactive thiol
  • Muscle contraction
  • Myosin conformation
  • Rhodamine

ASJC Scopus subject areas

  • General

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