A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements
A model for kinesin movement from nanometer-level movements of kinesin and cytoplasmic dynein and force measurements
复制标题
驱动蛋白运动的模型,来自驱动蛋白和细胞质动力蛋白的纳米级运动以及力测量
DOI:
10.1242/jcs.1991.supplement_14.27
复制
发表时间:
1991
影响因子:
4
通讯作者:
M. Sheetz
中科院分区:
文献类型:
--
作者:
S. Kuo;J. Gelles;E. Steuer;M. Sheetz
Summary Our detailed measurements of the movements of kinesin- and dynein-coated latex beads have revealed several important features of the motors which underlie basic mechanical aspects of the mechanisms of motor movements. Kinesin-coated beads will move along the paths of individual microtubule protofilaments with high fidelity and will pause at 4nm intervals along the microtubule axis under low ATP conditions. In contrast, cytoplasmic dynein-coated beads move laterally across many protofilaments as they travel along the microtubule, without any regular pauses, suggesting that the movements of kinesin-coated beads are not an artefact of the method. These kinesin bead movements suggest a model for kinesin movement in which the two heads walk along an individual protofilament in a hand-over-hand fashion. A free head would only be able to bind to the next forward tubulin subunit on the protofilament and its binding would pull off the trailing head to start the cycle again. This model is consistent with the observed cooperativity between the heads and with the movement by single dimeric molecules. Several testable predictions of the model are that kinesin should be able to bind to both alpha and beta tubulin and that the length of the neck region of the molecule should control the off-axis motility. In this article, we describe the technology for measuring nanometer-level movements and the force generated by the kinesin molecule.
影响因子:
64.8
作者:
ASHKIN, A;DZIEDZIC, JM;YAMANE, T
通讯作者:
YAMANE, T