期刊
SCIENCE
卷 295, 期 5556, 页码 844-848出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1063089
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The motor enzyme kinesin makes hundreds of unidirectional 8-nanometer steps without detaching from or freely sliding along the microtubule on which it moves. We investigated the kinesin stepping mechanism by immobilizing a Drosophila kinesin derivative through the carboxyl-terminal end of the neck coiled-coil domain and measuring orientations of microtubules moved by single enzyme molecules at submicromolar adenosine triphosphate concentrations. The kinesin-mediated microtubule-surface linkage was sufficiently torsionally stiff (greater than or equal to2.0+/-0.9 x 10(-20) Newton meters per radian(2)) that stepping by the hypothesized symmetric hand-over-hand mechanism would produce 180degrees rotations of the microtubule relative to the immobilized kinesin neck. In fact, there were no rotations, a finding that is inconsistent with symmetric hand-over-hand movement, An alternative inch-worm mechanism is consistent with our experimental results.
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