Article
- The EMBO Journal (2006) 25, 1795 - 1803
- doi:10.1038/sj.emboj.7601060
Published online: 6 April 2006
Subject Category:
Adaptability of myosin V studied by simultaneous detection of position and orientation
Sheyum Syed1,a, Gregory E Snyder1,a, Clara Franzini-Armstrong2,3, Paul R Selvin1,4 and Yale E Goldman2
- Department of Physics, University of Illinois, Urbana-Champaign, IL, USA
- Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, PA, USA
- Department of Cell and Developmental Biology, University of Pennsylvania, Philadelphia, PA, USA
- Center for Biophysics and Computational Biology, University of Illinois, Urbana-Champaign, IL, USA
Correspondence to:
Paul R Selvin, Loomis Lab of Physics, University of Illinois, 1110 W. Green St, Urbana, IL 61801, USA. Tel.: +1 217 244 3371; Fax: +1 217 244 7559; E-mail: selvin@uiuc.edu
Yale E Goldman, Pennsylvania Muscle Institute, University of Pennsylvania Medical Center, D700 Richards Bldg, 3700 Hamilton Walk, Philadelphia, PA 19104-6083, USA. Tel.: +1 215 898 4017; Fax: +1 215 898 2653; E-mail: goldmany@mail.med.upenn.edu
aThese authors contributed equally to this work
Received 2 September 2005; Accepted 2 March 2006
Abstract
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.
Keywords:
- fluorescence,
- head-to-head coordination,
- myosin V,
- polarization,
- single molecule
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