Cited by 177Microtubule and mitosis dynamicsProtein Structure and DynamicsForce Microscopy Techniques and Applications

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Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains

Hackney, David D.·1995·Nature

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Abstract

Studies of immobilized kinesin have shown that a single dimeric molecule can maintain contact with and drive sliding of a microtubule. In solution, however, native kinesin binds microtubules too weakly and hydrolyses ATP too slowly to produce the high sliding velocities seen in motility assay. This apparent inhibition in solution appears to be caused by the binding of kinesin's tail domains to its motor (head) domains in a folded conformation. DKH392, a construct containing two heads but no tails, has been shown to display both tight binding to microtubules and high ATPase rates. Furthermore, it retains one molecule of ADP per dimer when bound to microtubules, which could facilitate a 'hand-over-hand' mechanism for processive motion. Here we show that DKH392 hydrolyses more than 100 ATP molecules per diffusional encounter with a microtubule, even in the high-salt conditions encountered physiologically. This provides direct evidence that kinesin's activity is highly processive, with the motor remaining attached to a microtubule through many cycles of ATP hydrolysis.

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Hackney, D. D. Biophys. J. 68, s267–s270 (1995).
Hackney, D. D. & Nagy, J. M. Biophys. J. 68, a286 (1995).

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Authors: Hackney, D. D.
Affiliations: Carnegie Mellon University (US)
Corresponding author: Hackney, David D.
ORCID: Hackney, David D.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1995-10
Volume: 377
Issue: 6548
Pages: 448-450
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/377448a0
OpenAlex: W2049953608
Cited by: 177
References: 13
Citations by year: 2026: 4 · 2024: 7 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 1 · 2019: 4 · 2018: 1 · 2017: 4 · 2016: 4 · 2015: 5 · 2014: 2 · 2013: 1 · 2012: 5
FWCI: 4.03
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
Keywords: kinesin, microtubule sliding, ATP hydrolysis, processivity, microtubule binding, ADP binding, hand-over-hand mechanism, high-salt conditions, motility assay
MeSH terms: Adenosine Diphosphate, Adenosine Triphosphate, Hydrolysis, Microtubules, Kinesins

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Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains

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