Limping of Homodimeric Kinesin Motors

by: Ping Xie, Shuo-Xing Dou, Peng-Ye Wang

Journal of Molecular Biology, Vol. 366, No. 3. (23 February 2007), pp. 976-985.

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Abstract

Conventional kinesin, a homodimeric motor protein that transports cargo in various cells, walks limpingly along microtubule. Here, based on our previously proposed partially coordinated hand-over-hand model, we present a new mechanism for the limping behaviors of both wild-type and mutant kinesin homodimers. The limping is caused by different vertical forces acting on the heads in two successive steps during the processive movement of the dimer. From the model, various theoretical results, such as the dependences of the mean dwell time and dwell time ratio on the coiled-coil length and on the external load as well as the effect of vertical force on velocity, are in good agreement with previous experimental results. We predict that a high degree of limping will correlate strongly with a high sensitivity of ATP turnover rate to upwards force.

@article{citeulike:1281624, abstract = {Conventional kinesin, a homodimeric motor protein that transports cargo in various cells, walks limpingly along microtubule. Here, based on our previously proposed partially coordinated hand-over-hand model, we present a new mechanism for the limping behaviors of both wild-type and mutant kinesin homodimers. The limping is caused by different vertical forces acting on the heads in two successive steps during the processive movement of the dimer. From the model, various theoretical results, such as the dependences of the mean dwell time and dwell time ratio on the coiled-coil length and on the external load as well as the effect of vertical force on velocity, are in good agreement with previous experimental results. We predict that a high degree of limping will correlate strongly with a high sensitivity of ATP turnover rate to upwards force.}, author = {Xie, Ping and Dou, Shuo-Xing and Wang, Peng-Ye }, citeulike-article-id = {1281624}, journal = {Journal of Molecular Biology}, keywords = {kinesin, kinetics, model, motor}, month = {February}, number = {3}, pages = {976--985}, posted-at = {2007-05-07 09:28:45}, priority = {2}, title = {Limping of Homodimeric Kinesin Motors}, url = {http://www.sciencedirect.com/science/article/B6WK7-4M6XMJ3-5/2/59077319db17be5e10afc0b977438501}, volume = {366}, year = {2007} }

RIS record

TY - JOUR ID - citeulike:1281624 L3 - citeulike-article-id:1281624 TI - Limping of Homodimeric Kinesin Motors JF - Journal of Molecular Biology VL - 366 IS - 3 SP - 976 EP - 985 N2 - Conventional kinesin, a homodimeric motor protein that transports cargo in various cells, walks limpingly along microtubule. Here, based on our previously proposed partially coordinated hand-over-hand model, we present a new mechanism for the limping behaviors of both wild-type and mutant kinesin homodimers. The limping is caused by different vertical forces acting on the heads in two successive steps during the processive movement of the dimer. From the model, various theoretical results, such as the dependences of the mean dwell time and dwell time ratio on the coiled-coil length and on the external load as well as the effect of vertical force on velocity, are in good agreement with previous experimental results. We predict that a high degree of limping will correlate strongly with a high sensitivity of ATP turnover rate to upwards force. KW - kinesin KW - kinetics KW - model KW - motor AU - Xie, Ping AU - Dou, Shuo-Xing AU - Wang, Peng-Ye PY - 2007/02/23/ UR - http://www.sciencedirect.com/science/article/B6WK7-4M6XMJ3-5/2/59077319db17be5e10afc0b977438501 ER -

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