Different degrees of lever arm rotation control myosin step size.
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 approximately 90 degrees 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.
Institute for General Zoology and Genetics, Westfälische Wilhelms-University, Schlossplatz 5, 48149 Münster, Germany.
Danny
D
Köhler
Christine
C
Ruff
Edgar
E
Meyhöfer
Martin
M
Bähler
D000199:Actins / Q000737:chemistry*; D000818:Animals; D006367:HeLa Cells; D006801:Humans; D008968:Molecular Conformation; D020409:Molecular Motor Proteins / Q000737:chemistry; D015394:Molecular Structure; D008970:Molecular Weight; D009119:Muscle Contraction / Q000502:physiology; D009132:Muscles / Q000737:chemistry* / Q000502:physiology*; D009218:Myosins / Q000737:chemistry*; D051381:Rats; D012399:Rotation
D000199:Actins; D020409:Molecular Motor Proteins; D009218:Myosins