Three-dimensional structural dynamics of myosin V by single-molecule fluorescence polarization

Joseph N. Forkey, Margot E. Quinlan, M. Alexander Shaw, John E. T. Corrie and Yale E. Goldman ()
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Joseph N. Forkey: University of Pennsylvania
Margot E. Quinlan: University of Pennsylvania
M. Alexander Shaw: University of Pennsylvania
John E. T. Corrie: National Institute for Medical Research
Yale E. Goldman: University of Pennsylvania

Nature, 2003, vol. 422, issue 6930, 399-404

Abstract: Abstract The structural change that generates force and motion in actomyosin motility has been proposed to be tilting of the myosin light chain domain, which serves as a lever arm. Several experimental approaches have provided support for the lever arm hypothesis; however, the extent and timing of tilting motions are not well defined in the motor protein complex of functioning actomyosin. Here we report three-dimensional measurements of the structural dynamics of the light chain domain of brain myosin V using a single-molecule fluorescence polarization technique that determines the orientation of individual protein domains with 20–40-ms time resolution. Single fluorescent calmodulin light chains tilted back and forth between two well-defined angles as the myosin molecule processively translocated along actin. The results provide evidence for lever arm rotation of the calmodulin-binding domain in myosin V, and support a ‘hand-over-hand’ mechanism for the translocation of double-headed myosin V molecules along actin filaments. The technique is applicable to the study of real-time structural changes in other biological systems.

Date: 2003
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DOI: 10.1038/nature01529

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