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J. Biol. Chem., Vol. 276, Issue 18, 15117-15124, May 4, 2001
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From the To investigate the molecular functions of the
regions encoded by alternative exons from the single
Drosophila myosin heavy chain gene, we made the first
kinetic measurements of two muscle myosin isoforms that differ in all
alternative regions. Myosin was purified from the indirect flight
muscles of wild-type and transgenic flies expressing a major embryonic
isoform. The in vitro actin sliding velocity on the flight
muscle isoform (6.4 µm·s
Alternative Exon-encoded Regions of Drosophila Myosin
Heavy Chain Modulate ATPase Rates and Actin Sliding Velocity*
§,
,, Biology Department and Molecular Biology
Institute and the Department of Chemistry, San Diego State
University, San Diego, California 92182 and the ¶ Department of
Biology, University of York, P.O. Box 373, York YO1 5YW, United Kingdom
1 at 22 °C) is
among the fastest reported for a type II myosin and was 9-fold faster
than with the embryonic isoform. With smooth muscle tropomyosin bound
to actin, the actin sliding velocity on the embryonic isoform increased
6-fold, whereas that on the flight muscle myosin slightly decreased. No
difference in the step sizes of Drosophila and rabbit
skeletal myosins were found using optical tweezers, suggesting that the
slower in vitro velocity with the embryonic isoform is due
to altered kinetics. Basal ATPase rates for flight muscle myosin are
higher than those of embryonic and rabbit myosin. These differences
explain why the embryonic myosin cannot functionally substitute
in vivo for the native flight muscle isoform, and
demonstrate that one or more of the five myosin heavy chain alternative
exons must influence Drosophila myosin kinetics.
*
This work was supported by postdoctoral fellowships from the
National Institutes of Health and the American Heart Association Western affiliate (to D. M. S.); by a Biotechnology
and Biologicol Sciences Research Council, UK, research grant (to
J. C. S. and J. E. M., which supported M. L. B.); by NATO Collaborative Research Program Grant CRG940669 for
travel funds, which were instrumental in enabling much of the
collaborative work to be completed; and by National Institutes of
Health Grant GM32443 (to S. I. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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