The Effect of Monastrol on the Processive Motility of a Dimeric Kinesin-5 Head/Kinesin-1 Stalk Chimera
作者： Stefan Lakämper , Christina Thiede , André Düselder , Stefanie Reiter , Mikhail J. Korneev
DOI: 10.1016/J.JMB.2010.03.009
关键词:
摘要: Controlled activity of several kinesin motors is required for the proper assembly mitotic spindle. Eg5, a homotetrameric bipolar kinesin-5 from Xenopus laevis, can cross-link and slide anti-parallel microtubules apart by motility mechanism comprising diffusional directional modes. How this regulated, possibly tail domains opposing motors, poorly understood. In order to explore basic unregulated motor activity, we generated stably dimeric construct, Eg5Kin, consisting domain neck linker Eg5 coiled coil Drosophila melanogaster kinesin-1 (DmKHC). single-molecule assays, found chimera be highly processive. addition, studied effect kinesin-5-specific inhibitor monastrol using fluorescence assays. We that reduced length processive runs, but strikingly did not affect velocity. Quantitative analysis dose dependence suggests two bound molecules are an Eg5Kin dimer terminate run.
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