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EMBO Rep
2008 Aug 01;98:761-5. doi: 10.1038/embor.2008.96.
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Single-headed mode of kinesin-5.
Kaseda K, Crevel I, Hirose K, Cross RA.
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In most organisms, kinesin-5 motors are essential for mitosis and meiosis, where they crosslink and slide apart the antiparallel microtubule half-spindles. Recently, it was shown using single-molecule optical trapping that a truncated, double-headed human kinesin-5 dimer can step processively along microtubules. However, processivity is limited ( approximately 8 steps) with little coordination between the heads, raising the possibility that kinesin-5 motors might also be able to move by a nonprocessive mechanism. To investigate this, we engineered single-headed kinesin-5 dimers. We show that a set of these single-headed Eg5 dimers drive microtubule sliding at about 90% of wild-type velocity, indicating that Eg5 can slide microtubules by a mechanism in which one head of each Eg5head-pair is effectively redundant. On the basis of this, we propose a muscle-like model for Eg5-driven microtubule sliding in spindles in which most force-generating events are single-headed interactions and alternate-heads processivity is rare.
Adio,
Kinetic and mechanistic basis of the nonprocessive Kinesin-3 motor NcKin3.
2006, Pubmed
Adio,
Kinetic and mechanistic basis of the nonprocessive Kinesin-3 motor NcKin3.
2006,
Pubmed Allingham,
Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site.
2007,
Pubmed Alonso,
An ATP gate controls tubulin binding by the tethered head of kinesin-1.
2007,
Pubmed Carter,
Mechanics of the kinesin step.
2005,
Pubmed Cochran,
ATPase mechanism of Eg5 in the absence of microtubules: insight into microtubule activation and allosteric inhibition by monastrol.
2005,
Pubmed Crevel,
Monastrol stabilises an attached low-friction mode of Eg5.
2004,
Pubmed
,
Xenbase Crevel,
Coupled chemical and mechanical reaction steps in a processive Neurospora kinesin.
1999,
Pubmed Crevel,
What kinesin does at roadblocks: the coordination mechanism for molecular walking.
2004,
Pubmed Endres,
A lever-arm rotation drives motility of the minus-end-directed kinesin Ncd.
2006,
Pubmed Gilbert,
Alternating site mechanism of the kinesin ATPase.
1998,
Pubmed Hackney,
Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.
1994,
Pubmed Hancock,
Kinesin's processivity results from mechanical and chemical coordination between the ATP hydrolysis cycles of the two motor domains.
1999,
Pubmed Hancock,
Processivity of the motor protein kinesin requires two heads.
1998,
Pubmed Huang,
Drosophila kinesin minimal motor domain expressed in Escherichia coli. Purification and kinetic characterization.
1994,
Pubmed Kaseda,
Coordination of kinesin's two heads studied with mutant heterodimers.
2002,
Pubmed Kashina,
A bipolar kinesin.
1996,
Pubmed Korneev,
Load-dependent release limits the processive stepping of the tetrameric Eg5 motor.
2007,
Pubmed
,
Xenbase Krzysiak,
Getting in sync with dimeric Eg5. Initiation and regulation of the processive run.
2008,
Pubmed Krzysiak,
Dimeric Eg5 maintains processivity through alternating-site catalysis with rate-limiting ATP hydrolysis.
2006,
Pubmed Lockhart,
Origins of reversed directionality in the ncd molecular motor.
1994,
Pubmed Lockhart,
Kinetics and motility of the Eg5 microtubule motor.
1996,
Pubmed
,
Xenbase Ma,
Interacting head mechanism of microtubule-kinesin ATPase.
1997,
Pubmed Mori,
How kinesin waits between steps.
2007,
Pubmed Nishiyama,
Chemomechanical coupling of the forward and backward steps of single kinesin molecules.
2002,
Pubmed Rosenfeld,
Stepping and stretching. How kinesin uses internal strain to walk processively.
2003,
Pubmed Tomishige,
Conversion of Unc104/KIF1A kinesin into a processive motor after dimerization.
2002,
Pubmed Valentine,
Individual dimers of the mitotic kinesin motor Eg5 step processively and support substantial loads in vitro.
2006,
Pubmed Veigel,
Load-dependent kinetics of myosin-V can explain its high processivity.
2005,
Pubmed
