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Related Experiment Videos

Processivity of chimeric class V myosins.

Elena B Krementsova1, Alex R Hodges, Hailong Lu

  • 1Department of Molecular Physiology and Biophysics, University of Vermont, 149 Beaumont Avenue, Burlington, VT 05405, USA.

The Journal of Biological Chemistry
|December 27, 2005
PubMed
Summary
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Myosin V

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Unconventional myosin V is crucial for intracellular cargo transport, taking long steps along actin filaments.
  • Processive run length is key for myosin V's long-distance cargo movement.
  • Understanding structural features influencing run length is vital for cell biology.

Purpose of the Study:

  • To investigate the structural determinants of myosin V processive run length.
  • To analyze the properties of chimeric myosins combining mouse and yeast (Myo4p) class V myosins.
  • To elucidate the role of specific myosin V regions, particularly loop 2, in actin binding and processivity.

Main Methods:

  • Construction and analysis of chimeric myosin V constructs, including Y-MD (yeast motor domain on mouse myosin V neck and rod).

Related Experiment Videos

  • Measurement of myosin V run lengths at varying salt concentrations.
  • Biochemical assays, including steady-state ATPase assays, to determine kinetic parameters like K(m) for actin.

    • Main Results:

    • A Y-MD chimera exhibited longer run lengths than wild-type mouse myosin V at low salt.
    • Mouse myosin V run length showed minimal salt dependence, while Y-MD's decreased steeply with ionic strength.
    • Yeast loop 2, when incorporated into mouse myosin V, also showed steep salt dependence and a higher K(m) for actin.
    • Yeast loop 2 has no net charge, contrasting with the +6 charge of wild-type loop 2.

    Conclusions:

    • A positively charged loop 2 is important for maintaining myosin V processivity at physiological ionic strength.
    • High affinity for actin, influenced by loop 2 charge, is critical for sustained processive movement.
    • Structural variations in loop 2 significantly impact myosin V's ability to maintain long run lengths.