The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Highly processive microtubule-stimulated ATP hydrolysis by dimeric kinesin head domains
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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“the k cat value was smaller than that reported for kinesin-1 (ϳ50 s Ϫ1 ) (33,34) but was similar to those of Ncd, Kar3, and Eg5.”
From Diffusion and Directed Movement (2008) · cites this paper as [33]
Citations
Cites
Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993
Direct observation of kinesin stepping by optical trapping interferometry
Svoboda, K., Schmidt, C. F., Schnapp, B. J., & Block, S. M. (1993) · Nature · doi:10.1038/365721a0 · Cited by 1,910
Bead movement by single kinesin molecules studied with optical tweezers
Block, S. M., Goldstein, L. S. B., & Schnapp, B. J. (1990) · Nature · doi:10.1038/348348a0 · Cited by 1,038
Movement of microtubules by single kinesin molecules
Howard, J., Hudspeth, A. J., & Vale, R. D. (1989) · Nature · doi:10.1038/342154a0 · Cited by 885
Evidence for alternating head catalysis by kinesin during microtubule-stimulated ATP hydrolysis.
Hackney, D. D. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.15.6865 · Cited by 351
Self-citationPathway of processive ATP hydrolysis by kinesin
Gilbert, S. P., Webb, M. R., Brune, M., & Johnson, K. A. (1995) · Nature · doi:10.1038/373671a0 · Cited by 252
Kinesin ATPase: rate-limiting ADP release
Hackney, D. D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.17.6314 · Cited by 239
Self-citationKinesin undergoes a 9 S to 6 S conformational transition
Hackney, D. D., Levitt, J. D., & Suhan, J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42499-4 · Cited by 175
Self-citationHuang, T. G., & Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34033-4 · Cited by 174
Self-citationHuang, T. G., Suhan, J. P., & Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34034-6 · Cited by 90
Self-citationA kinetic study of the kinesin ATPase.
Sadhu, A., & Taylor, E. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49917-1 · Cited by 73
Hackney, D. D. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34035-8 · Cited by 68
Self-citationNucleotide-free Kinesin Hydrolyzes ATP with Burst Kinetics
Hackney, D. D., Malik, A. S., & Wright, K. W. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71570-6 · Cited by 40
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Research works printed but not linked: 2
- Hackney, D. D. Biophys. J. 68, s267–s270 (1995).
- Hackney, D. D. & Nagy, J. M. Biophys. J. 68, a286 (1995).
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Erbaş-Çakmak, S., Leigh, D. A., McTernan, C. T., & Nussbaumer, A. L. (2015) · Chemical Reviews · doi:10.1021/acs.chemrev.5b00146 · Cited by 2,016
Schliwa, M., & Woehlke, G. (2003) · Nature · doi:10.1038/nature01601 · Cited by 1,089
Kinesin hydrolyses one ATP per 8-nm step
Schnitzer, M. J., & Block, S. M. (1997) · Nature · doi:10.1038/41111 · Cited by 771
Direct observation of single kinesin molecules moving along microtubules
Vale, R. D., Funatsu, T., Pierce, D. W., Romberg, L., Harada, Y., & Yanagida, T. (1996) · Nature · doi:10.1038/380451a0 · Cited by 711
Force production by single kinesin motors
Schnitzer, M. J., Visscher, K., & Block, S. M. (2000) · Nature Cell Biology · doi:10.1038/35036345 · Cited by 572
Metadata
- Authors
- Hackney, D. D.
- Affiliations
- Carnegie Mellon University (US)
- Corresponding author
- Hackney, David D.
- ORCID
- Hackney, David D.
- Venue
- Nature
- Published
- 1995-10
- Volume
- 377
- Issue
- 6548
- Pages
- 448-450
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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