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          Institute: MPI für molekulare Zellbiologie und Genetik     Collection: Publikationen MPI-CBG 2010-arch     Display Documents



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ID: 546699.0, MPI für molekulare Zellbiologie und Genetik / Publikationen MPI-CBG 2010-arch
Single-molecule stepping and structural dynamics of myosin X.
Authors:Sun, Yujie; Sato, Osamu; Ruhnow, Felix; Arsenault, Mark E; Ikebe, Mitsuo; Goldman, Yale E
Date of Publication (YYYY-MM-DD):2010
Title of Journal:Nature Structural & Molecular Biology
Volume:17
Issue / Number:4
Start Page:485
End Page:491
Copyright:not available
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Myosin X is an unconventional myosin with puzzling motility properties. We studied the motility of dimerized myosin X using the single-molecule fluorescence techniques polTIRF, FIONA and Parallax to measure the rotation angles and three-dimensional position of the molecule during its walk. It was found that Myosin X steps processively in a hand-over-hand manner following a left-handed helical path along both single actin filaments and bundles. Its step size and velocity are smaller on actin bundles than individual filaments, suggesting myosin X often steps onto neighboring filaments in a bundle. The data suggest that a previously postulated single alpha-helical domain mechanically extends the lever arm, which has three IQ motifs, and either the neck-tail hinge or the tail is flexible. These structural features, in conjunction with the membrane- and microtubule-binding domains, enable myosin X to perform multiple functions on varied actin structures in cells.
External Publication Status:published
Document Type:Article
Version Comment:Automatic journal name synchronization
Communicated by:nn
Affiliations:MPI für molekulare Zellbiologie und Genetik
Identifiers:LOCALID:4409
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