期刊
FEBS LETTERS
卷 569, 期 1-3, 页码 54-58出版社
WILEY
DOI: 10.1016/j.febslet.2004.05.050
关键词
kinesin; processivity; optical trap; myosin tail; myosin filament; myosin self-assembly
The rat kinesin motor domain was fused at residues 433, 411, 376 or 367, respectively, to the C-terminal 1185, 1187, 1197 or 1185 residues of the brush border myosin tail. In motility assays, K433myt and K411myt, which preserve the head-proximal kinesin hinge, and K367myt, which deletes it, drove rapid microtubule sliding (similar to0.6 mums(-1)) that was optimal when the head-pairs were spaced apart by adding 1:1 headless myosin tails. K376myt, which partially deletes the head-proximal hinge, showed poor motility in sliding assays but wild type processivity, velocity and stall force in single molecule optical trapping. Accordingly, the head-proximal kinesin hinge is functionally dispensable. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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