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Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
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Myosin as a potential redox-sensor: an in vitro study.

Chiara Passarelli1, Stefania Petrini, Anna Pastore

  • 1Molecular Medicine Unit, Children's Hospital and Research Institute Bambino Gesù, Department of Biology, University of Rome Roma Tre, P.za S. Onofrio, 4, Rome, 00165, Italy.

Journal of Muscle Research and Cell Motility
|September 10, 2008
PubMed
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Skeletal muscle force production relies on redox balance. Myosin protein glutathionylation impacts muscle structure and function, potentially acting as a cellular redox sensor.

Area of Science:

  • Muscle physiology
  • Redox biology
  • Protein biochemistry

Background:

  • Skeletal muscle force production requires balanced redox status.
  • Free radicals in skeletal muscle are involved in physiological processes like excitation-contraction coupling.
  • Protein glutathionylation regulates protein redox status and signal transduction.

Purpose of the Study:

  • To investigate the effect of glutathionylation on myosin.
  • To identify potential sites of glutathione binding on myosin.
  • To understand how myosin glutathionylation impacts its structure and function.

Main Methods:

  • In vitro glutathionylation of myosin.
  • MALDI-TOF analysis to identify glutathione binding sites.
  • Measurement of fluorescence quantum yield and susceptibility to proteolytic cleavage.

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  • Assessment of myosin ATPase activity under varying GSSG redox balance.

    • Main Results:

    • Myosin is sensitive to in vitro glutathionylation.
    • Three potential glutathione binding sites were identified on myosin, two on the myosin head.
    • Glutathionylation decreased myosin's fluorescence quantum yield and increased its susceptibility to proteolytic cleavage.
    • Myosin ATPase activity was modulated by glutathionylation, dependent on the GSSG redox balance.

    Conclusions:

    • Myosin glutathionylation significantly impacts protein structure and function.
    • Glutathionylation may be a mechanism for glutathione to modulate sarcomere function based on tissue redox state.
    • Myosin may function as a redox sensor in muscle cells.