Source:http://linkedlifedata.com/resource/pubmed/id/21680740
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
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pubmed:dateCreated |
2011-8-15
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pubmed:abstractText |
Kar3Cik1 is a Saccharomyces cerevisiae kinesin-14 that functions to shorten cytoplasmic microtubules (MTs) during yeast mating yet maintains mitotic spindle stability by cross-linking anti-parallel interpolar MTs. Kar3 contains both an ATP- and a MT-binding site, yet there is no evidence of a nucleotide-binding site in Cik1. Presteady-state and steady-state kinetic experiments were pursued to define the regulation of Kar3Cik1 interactions with the MT lattice expected during interpolar MT cross-linking. The results reveal that association of Kar3Cik1 with the MT occurs at 4.9 ?M(-1) s(-1), followed by a 5-s(-1) structural transition that limits ADP release from the Kar3 head. Mant-ATP binding occurred at 2.1 ?M(-1) s(-1), and the pulse-chase experiments revealed an ATP-promoted isomerization at 69 s(-1). ATP hydrolysis was observed as a rapid step at 26 s(-1) and was required for the Kar3Cik1 motor to detach from MT. The conformational change at 5 s(-1) that occurred after Kar3Cik1 MT association and prior to ADP release was hypothesized to be the rate-limiting step for steady-state ATP turnover. We propose a model in which Kar3Cik1 interacts with the MT lattice through an alternating cycle of Cik1 MT collision followed by Kar3 MT binding with head-head communication between Kar3 and Cik1 modulated by the Kar3 nucleotide state and intramolecular strain.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/CIK1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/KAR3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microtubule-Associated Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
19
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pubmed:volume |
286
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29261-72
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pubmed:dateRevised |
2011-10-19
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pubmed:meshHeading |
pubmed-meshheading:21680740-Adenosine Triphosphatases,
pubmed-meshheading:21680740-Binding Sites,
pubmed-meshheading:21680740-Microtubule Proteins,
pubmed-meshheading:21680740-Microtubule-Associated Proteins,
pubmed-meshheading:21680740-Microtubules,
pubmed-meshheading:21680740-Mitotic Spindle Apparatus,
pubmed-meshheading:21680740-Models, Biological,
pubmed-meshheading:21680740-Protein Binding,
pubmed-meshheading:21680740-Saccharomyces cerevisiae,
pubmed-meshheading:21680740-Saccharomyces cerevisiae Proteins
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pubmed:year |
2011
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pubmed:articleTitle |
Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.
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pubmed:affiliation |
Department of Biology and the Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York 12180, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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