help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH

Biophys. J. BioFAST: First Published January 6, 2006. doi:10.1529/biophysj.105.075184
© 2006 by the Biophysical Society.


A more recent version of this article appeared on April 1, 2006.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow All Versions of this Article:
biophysj.105.075184v1
90/7/2427    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Swank, D. M
Right arrow Articles by Maughan, D. W
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Swank, D. M
Right arrow Articles by Maughan, D. W

MUSCLE AND CONTRACTILITY

An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics

Douglas M Swank 1*, Joan Braddock 2, Waylon Brown 2, Heather Lesage 2, Sanford I Bernstein 3 and David W Maughan 2

1 Rensselaer Polytechnic Institute
2 University of Vermont
3 San Diego State University

* To whom correspondence should be addressed. E-mail: swankd{at}rpi.edu.

Submitted on September 27, 2005
Revised on November 17, 2005
Accepted on 28 November 2005


   Abstract
We examined the importance of alternative versions of a region near the ATP binding site of Drosophila myosin heavy chain (MHC) on muscle mechanical properties. Previously, we exchanged two versions of this region (encoded by alternative exon 7s) between the indirect flight muscle myosin isoform (IFI) and an embryonic myosin isoform (EMB) and found, surprisingly, that in vitro solution actin-activated ATPase rates were increased (higher Vmax) by both exon exchanges. Here we examined the effect of increased ATPase rate on indirect flight muscle (IFM) fiber mechanics and Drosophila locomotion. IFM expressing EMB with the exon 7a domain replaced by the IFM specific exon 7d domain (EMB-7d) exhibited 3.2-fold greater maximum oscillatory power (Pmax) and 1.5-fold greater optimal frequency of power generation (fmax) versus fibers expressing EMB. In contrast, IFM expressing IFI with the exon 7d region replaced by the EMB exon 7a region (IFI-7a), showed no change in Pmax, fmax, step response, or isometric muscle properties compared to native IFI fibers. A slight decrement in IFI-7a flight ability was observed, suggesting a negative influence of the increased ATPase rate on Drosophila locomotion, perhaps due to energy supply constraints. Our results show that exon 7 plays a substantial role in establishing fiber speed and flight performance, and that the limiting step that sets ATPase rate in Drosophila myosin has little to no direct influence in setting fmax for fast muscle fiber types.

Key Words: actomyosin, cross-bridge, flight, muscle mechanics, wing beat frequency




This article has been cited by other articles:


Home page
Biophys. JHome page
B. M. Palmer, T. Suzuki, Y. Wang, W. D. Barnes, M. S. Miller, and D. W. Maughan
Two-State Model of Acto-Myosin Attachment-Detachment Predicts C-Process of Sinusoidal Analysis
Biophys. J., August 1, 2007; 93(3): 760 - 769.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2006 by the Biophysical Society.