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PMID: 7854446 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Pathway of processive ATP hydrolysis by kinesin.

Nature ·Vol. 373 ·No. 6516 ·1995-02-23 ·Pages 671-6

Gilbert SP, Webb MR, Brune M, Johnson KA

Abstract

Direct measurement of the kinetics of kinesin dissociation from microtubules, the release of phosphate and ADP from kinesin, and rebinding of kinesin to the microtubule have defined the mechanism for the kinesin ATPase cycle. The processivity of ATP hydrolysis is ten molecules per site at low salt concentration but is reduced to one ATP per site at higher salt concentration. Kinesin dissociates from the microtubule after ATP hydrolysis. This step is rate-limiting. The subsequent rebinding of kinesin-ADP to the microtubule is fast, so kinesin spends only a small fraction of its duty cycle in the dissociated state. These results provide an explanation for the motility differences between skeletal myosin and kinesin.

MeSH Terms
Adenosine Diphosphate/metabolism Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Animals Drosophila Escherichia coli Hydrolysis Kinesins/metabolism Kinetics Microtubules/metabolism Organophosphates/metabolism Peptide Fragments/genetics,metabolism Recombinant Proteins
Chemicals
Organophosphates Peptide Fragments Recombinant Proteins Adenosine Diphosphate Adenosine Triphosphate Adenosine Triphosphatases Kinesins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Gilbert S P
Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park 16802.
Webb M R
Brune M
Johnson K A
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23 references, click to expand
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Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-02-23
Pages
671-6
Language
English
Region
England
NLM ID
0410462
PMCID
PMC1855160
Subset
IM
Grants
NIGMS NIH HHS · R01 GM026726 · United States
Corrections
CommentIn
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