Abstract:
:Controlled activity of several kinesin motors is required for the proper assembly of the mitotic spindle. Eg5, a homotetrameric bipolar kinesin-5 from Xenopus laevis, can cross-link and slide anti-parallel microtubules apart by a motility mechanism comprising diffusional and directional modes. How this mechanism is regulated, possibly by the tail domains of the opposing motors, is poorly understood. In order to explore the basic unregulated kinesin-5 motor activity, we generated a stably dimeric kinesin-5 construct, Eg5Kin, consisting of the motor domain and neck linker of Eg5 and the neck coiled coil of Drosophila melanogaster kinesin-1 (DmKHC). In single-molecule motility assays, we found this chimera to be highly processive. In addition, we studied the effect of the kinesin-5-specific inhibitor monastrol using single-molecule fluorescence assays. We found that monastrol reduced the length of processive runs, but strikingly did not affect velocity. Quantitative analysis of monastrol dose dependence suggests that two bound monastrol molecules are required to be bound to an Eg5Kin dimer to terminate a run.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Lakämper S,Thiede C,Düselder A,Reiter S,Korneev MJ,Kapitein LC,Peterman EJ,Schmidt CFdoi
10.1016/j.jmb.2010.03.009subject
Has Abstractpub_date
2010-05-28 00:00:00pages
1-8issue
1eissn
0022-2836issn
1089-8638pii
S0022-2836(10)00247-0journal_volume
399pub_type
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