Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling

Miller, Becky M. and Nyitrai, Miklos and Bernstein, Sanford I. and Geeves, Michael A. (2003) Kinetic analysis of Drosophila muscle myosin isoforms suggests a novel mode of mechanochemical coupling. Journal of Biological Chemistry, 278 (50). pp. 50293-50300. ISSN 0021-9258. (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1074/jbc.M308318200

Abstract

The molecular mechanism of myosin function was addressed by measuring transient kinetic parameters of naturally occurring and chimeric Drosophila muscle myosin isoforms. We assessed the native embryonic isoform, the native indirect flight muscle isoform, and two chimeric isoforms containing converter domains exchanged between the indirect flight muscle and embryonic isoforms. Myosin was purified from the indirect flight muscles of transgenic flies, and S1 was produced by alpha-chymotryptic digestion. Previous studies in vertebrate and scallop myosins have shown a correlation between actin filament velocity in motility assays and cross-bridge detachment rate, specifically the rate of ADP release. In contrast, our study showed no correlation between the detachment rate and actin filament velocity in Drosophila myosin isoforms and further that the converter domain does not significantly influence the biochemical kinetics governing the detachment of myosin from actin. We suggest that evolutionary pressure on a single muscle myosin gene may maintain a fast detachment rate in all isoforms. As a result, the attachment rate and completion of the power stroke or the equilibrium between actin.myosin.ADP states may define actin filament velocity for these myosin isoforms.

Item Type: Article
Additional information: 0021-9258 (Print) Journal Article
Uncontrolled keywords: Actins/chemistry Adenosine Triphosphate/chemistry Adenosinetriphosphatase/chemistry Amino Acid Sequence Animals Animals, Genetically Modified Ca(2+) Mg(2+)-ATPase/chemistry Chymotrypsin/metabolism Dose-Response Relationship, Drug Drosophila melanogaster/*metabolism Electrophoresis, Polyacrylamide Gel Kinetics Light Magnesium/chemistry Models, Chemical Models, Molecular Molecular Sequence Data Muscle, Skeletal/metabolism Muscles/*metabolism Myosins/*chemistry/metabolism Photolysis Protein Binding Protein Isoforms Protein Structure, Secondary Protein Structure, Tertiary Rabbits Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Scattering, Radiation Sequence Homology, Amino Acid Time Factors
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Michael Geeves
Date Deposited: 14 Mar 2009 16:14
Last Modified: 29 Apr 2014 08:18
Resource URI: http://kar.kent.ac.uk/id/eprint/13193 (The current URI for this page, for reference purposes)
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