期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 4, 页码 485-U131出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1785
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资金
- US National Science Foundation Nanoscale Science and Engineering Center through the Nano/Bio Interface Center [DMR-0425780]
- NIH [GM086352]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM086352] Funding Source: NIH RePORTER
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.
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