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Published 28 April 2003. doi:10.1083/jcb.200212039
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© The Rockefeller University Press, 0021-9525/2003/4/237 $5.00
The Journal of Cell Biology, Volume 161, Number 2, 237-241

Report

 Different degrees of lever arm rotation control myosin step size

Danny Köhler1, Christine Ruff2, Edgar Meyhöfer2 and Martin Bähler1

1 Institute for General Zoology and Genetics, Westfälische Wilhelms-University, 48149 Münster, Germany
2 Molecular and Cellular Physiology, Medical School Hannover, 30625 Hannover, Germany

Address correspondence to Martin Bähler, Institute for General Zoology and Genetics, Westfälische Wilhelms-University, Schlossplatz 5, 48149 Münster, Germany. Tel.: 49-251-83-23874. Fax: 49-251-83-24723. E-mail: baehler{at}uni-muenster.de; or Edgar Meyhöfer, Department of Mechanical Engineering, University of Michigan, 2350 Hayward Street, Ann Arbor, MI 48109-2125. Tel.: (734) 647-7856. Fax: (734) 615-6647. E-mail: meyhofer{at}umich.edu

Myosins are actin-based motors that are generally believed to move by amplifying small structural changes in the core motor domain via a lever arm rotation of the light chain binding domain. However, the lack of a quantitative agreement between observed step sizes and the length of the proposed lever arms from different myosins challenges this view. We analyzed the step size of rat myosin 1d (Myo1d) and surprisingly found that this myosin takes unexpectedly large steps in comparison to other myosins. Engineering the length of the light chain binding domain of rat Myo1d resulted in a linear increase of step size in relation to the putative lever arm length, indicative of a lever arm rotation of the light chain binding domain. The extrapolated pivoting point resided in the same region of the rat Myo1d head domain as in conventional myosins. Therefore, rat Myo1d achieves its larger working stroke by a large calculated ~90° rotation of the light chain binding domain. These results demonstrate that differences in myosin step sizes are not only controlled by lever arm length, but also by substantial differences in the degree of lever arm rotation.

Key Words: myosin 1d; motor molecule; calmodulin; IQ motif; single molecule measurement

C. Ruff's present address is European Patent Office, D-80331 Munich, Germany.

E. Meyhöfer's present address is Department of Mechanical Engineering, University of Michigan, Ann Arbor, MI 48109-2125.

* Abbreviation used in this paper: Myo1d, myosin 1d.


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