Overlapping Hand-over-Hand Mechanism of Single Molecular Motility of Cytoplasmic Dynein

Structural differences between dynein and kinesin suggest a unique molecular mechanism of dynein motility. Measuring the mechanical properties of a single molecule of dynein is crucial for revealing the mechanisms underlying its movement. We measured the step size and force produced by single molecu...

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Bibliographic Details
Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 103; no. 15; pp. 5741 - 5745
Main Authors:	Toba, Shiori, Watanabe, Tomonobu M., Yamaguchi-Okimoto, Lisa, Toyoshima, Yoko Yano, Higuchi, Hideo
Format:	Journal Article
Language:	English
Published:	United States National Academy of Sciences 11-04-2006
Subjects:	Adenosine Triphosphate - metabolism Adenylyl Imidodiphosphate - pharmacology Animals Biological Sciences Biophysics Brain - enzymology Cytoplasm - enzymology Dyneins - chemistry Dyneins - metabolism Fluorescence Histograms Kinesin - metabolism Kinetics Lasers Low speed Microtubules Microtubules - enzymology Molecules Nanotechnology Proteins Stall Stiffness Swine Temporal resolution Velocity
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Summary:	Structural differences between dynein and kinesin suggest a unique molecular mechanism of dynein motility. Measuring the mechanical properties of a single molecule of dynein is crucial for revealing the mechanisms underlying its movement. We measured the step size and force produced by single molecules of active cytoplasmic dynein by using an optical trap and fluorescence imaging with a high temporal resolution. The velocity of dynein movement, 800 nm/s, is consistent with that reported in cells. The maximum force of 7-8 pN was independent of the ATP concentration and similar to that of kinesin. Dynein exhibited forward and occasional backwards steps of ≈8 nm, independent of load. It is suggested that the large dynein heads take 16-nm steps by using an overlapping hand-over-hand mechanism.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: Kansai Advanced Research Center, National Institute of Information and Communications Technology, Kobe, Hyogo 651-2492, Japan. Author contributions: S.T., Y.Y.T., and H.H. designed research; S.T., T.M.W., L.Y.-O., Y.Y.T., and H.H. performed research; S.T. and H.H. contributed new reagents/analytic tools; S.T., T.M.W., L.Y.-O., Y.Y.T., and H.H. analyzed data; and S.T., Y.Y.T., and H.H. wrote the paper. Edited by James A. Spudich, Stanford University School of Medicine, Stanford, CA, and approved February 11, 2006
ISSN:	0027-8424 1091-6490
DOI:	10.1073/pnas.0508511103