Adaptability of myosin V studied by simultaneous detection of position and orientation

Sheyum Syed, Gregory E. Snyder, Clara Franzini-Armstrong, Paul R. Selvin, Yale E. Goldman

Research output: Contribution to journalArticlepeer-review


We studied the structural dynamics of chicken myosin V by combining the localization power of fluorescent imaging with one nanometer accuracy (FIONA) with the ability to detect angular changes of a fluorescent probe. The myosin V was labeled with bifunctional rhodamine on one of its calmodulin light chains. For every 74 nm translocation, the probe exhibited two reorientational motions, associated with alternating smaller and larger translational steps. Molecules previously identified as stepping alternatively 74-0 nm were found to actually step 64-10 nm. Additional tilting often occurred without full steps, possibly indicating flexibility of the attached myosin heads or probing of their vicinity. Processive myosin V molecules sometimes shifted from the top to the side of actin, possibly to avoid an obstacle. The data indicate marked adaptability of this molecular motor to a nonuniform local environment and provide strong support for a straight-neck model of myosin V in which the lever arm of the leading head is tilted backwards at the prepowerstoke angle.

Original languageEnglish (US)
Pages (from-to)1795-1803
Number of pages9
JournalEMBO Journal
Issue number9
StatePublished - May 3 2006


  • Fluorescence
  • Head-to-head coordination
  • Myosin V
  • Polarization
  • Single molecule

ASJC Scopus subject areas

  • General Neuroscience
  • Molecular Biology
  • General Biochemistry, Genetics and Molecular Biology
  • General Immunology and Microbiology


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