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Fine tuning a molecular motor: The location of alternative domains in the drosophila myosin head

Academic Article
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Overview

authors

  • Bernstein, S. I.
  • Milligan, Ronald

publication date

  • August 1997

journal

  • Journal of Molecular Biology  Journal

abstract

  • Myosin isoform sequence variation is likely critical for generating differences in contraction velocity and force production exhibited by the various skeletal muscles in an animal. To examine how myosin heavy chain (MHC) isoform diversity could affect physiological function, we studied the locations of structural differences in the motor domains of muscle MHCs from Drosophila melanogaster. Drosophila has only one muscle Mhc gene. Isoform variation is achieved by alternative splicing of a limited number of exons, clearly delineating the domains of MHC that are critical for muscle-specific functions. There are four alternative regions that contribute to the motor domain of Drosophila myosin. We used the X-ray structure of chicken skeletal S1 as a framework to examine the locations of these four regions. One lies near the ATP-binding pocket in a position where amino acid changes might be expected to modulate entry or exit of the nucleotide. Interestingly, the other three are clustered at the distal end of the molecule, surrounding the reactive cysteine SH1 and the pivot point about which the light chain-containing region swings. These observations underscore the importance of this region, distant from the site of ATP entry and the actin binding interface, as a part of the molecule where modulation of function can be achieved.

subject areas

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Chickens
  • Crystallography, X-Ray
  • Drosophila melanogaster
  • Exons
  • Models, Molecular
  • Molecular Sequence Data
  • Muscle, Skeletal
  • Muscles
  • Myosin Heavy Chains
  • Myosin Subfragments
  • Protein Structure, Secondary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
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Research

keywords

  • alternative RNA splicing
  • muscle
  • myosin heavy chain
  • protein function
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1006/jmbi.1997.1160

PubMed ID

  • 9300050
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Additional Document Info

start page

  • 1

end page

  • 6

volume

  • 271

issue

  • 1

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