Cited by 175Microtubule and mitosis dynamicsProtein Structure and DynamicsEnzyme Structure and Function

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Kinesin undergoes a 9 S to 6 S conformational transition

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Hackney, D.D., Levitt, J.D., Suhan, J·1992·Journal of Biological Chemistry

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Abstract

Addition of NaCl or KCl in the presence of 50 nM ATP induces a shift in the sedimentation coefficient (apparent S20,w) of kinesin from 9.4 S at low ionic strength to 6.5 S at high ionic strength. The midpoint for the transition occurs at ionic strength values of 0.39, 0.25, and 0.18 for pH values of 6.3, 6.9, and 8.3, respectively. Gel filtration experiments indicate that the transition to the 6.5 S species is accompanied by a decrease in the diffusion coefficient. Under all conditions which were tested, the 64-kDa beta subunits comigrate with the 120-kDa alpha subunits without any evidence for dissociation of the alpha 2 beta 2 complex. These results are consistent with the change in sedimentation coefficient being due to a conformational transition between a folded form at low ionic strength and an extended form at high ionic strength. This conformational transition is not significantly affected by the nature of the nucleotide bound at the active site since similar results are obtained both in the presence of excess EDTA, which removes the bound ADP, and after replacement of the bound ADP with adenosine 5'-(beta,gamma-imino)triphosphate. The alpha 2 form of kinesin, which lacks the beta subunits, undergoes a similar transition between a 6.7 S form at low ionic strength and a 5.1 S form at high ionic strength with a midpoint for the transition at an ionic strength of 0.5 at pH 6.9. Electron microscopic observation also indicates a transition between a folded conformation at low ionic strength and an extended conformation at high ionic strength for both the alpha 2 beta 2 and alpha 2 species.

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LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961
Substructure of the myosin molecule
Weeds, A. G., & Lowey, S. (1971) · Journal of Molecular Biology · doi:10.1016/0022-2836(71)90074-x · Cited by 1,067
[7] Preparation of myosin and its subfragments from rabbit skeletal muscle
Margossian, S. S., & Lowey, S. (1982) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(82)85009-x · Cited by 981
Substructure of the myosin molecule
Lowey, S., Slayter, H. S., Weeds, A. G., & Baker, H. (1969) · Journal of Molecular Biology · doi:10.1016/0022-2836(69)90483-5 · Cited by 779
A new protein of the thick filaments of vertebrate skeletal myofibrils
Offer, G., Moos, C., & Starr, R. (1973) · Journal of Molecular Biology · doi:10.1016/0022-2836(73)90055-7 · Cited by 629
Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration
Hirokawa, N., Pfister, K. K., Yorifuji, H., Wagner, M. C., Brady, S. T., & Bloom, G. S. (1989) · Cell · doi:10.1016/0092-8674(89)90691-0 · Cited by 477
A New Calibration Procedure for Gel Filtration Columns
Ackers, G. K. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)95955-7 · Cited by 413
A three-domain structure of kinesin heavy chain revealed by DNA sequence and microtubule binding analyses
Yang, J. T., Laymon, R. A., & Goldstein, L. S. B. (1989) · Cell · doi:10.1016/0092-8674(89)90692-2 · Cited by 395
A bent monomeric conformation of myosin from smooth muscle.
Trybus, K. M., Huiatt, T. W., & Lowey, S. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.20.6151 · Cited by 300
Native structure and physical properties of bovine brain kinesin and identification of the ATP-binding subunit polypeptide
Bloom, G. S., Wagner, M. C., Pfister, K. K., & Brady, S. T. (1988) · Biochemistry · doi:10.1021/bi00409a043 · Cited by 284

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DeBerg, H. A., Blehm, B. H., Sheung, J., Thompson, A. R., Bookwalter, C. S., Torabi, S. F., Schroer, T. A., Berger, C. L., Lu, Y., Trybus, K. M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515510 · Cited by 52
Kinesin-related proteins in eukaryotic flagella
Fox, L. A., Sawin, K. E., & Sale, W. S. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.6.1545 · Cited by 51
Diffusive Movement of Processive Kinesin‐1 on Microtubules
Lu, H., Ali, M. Y., Bookwalter, C. S., Warshaw, D. M., & Trybus, K. M. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00964.x · Cited by 48
Importance of a flexible hinge near the motor domain in kinesin‐driven motility
Grummt, M., Woehlke, G., Henningsen, U., Fuchs, S., Schleicher, M., & Schliwa, M. (1998) · The EMBO Journal · doi:10.1093/emboj/17.19.5536 · Cited by 48
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Sanger, A., Yip, Y. Y., Randall, T. S., Pernigo, S., Steiner, R. A., & Dodding, M. P. (2017) · Journal of Cell Science · doi:10.1242/jcs.198267 · Cited by 47
[14] Assaying processive movement of kinesin by fluorescence microscopy
Pierce, D. W., & Vale, R. D. (1998) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(98)98016-8 · Cited by 48
One axon, many kinesins: What's the logic?
Mureşan, V. (2000) · Journal of Neurocytology · doi:10.1023/a:1010943424272 · Cited by 46
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Lakämper, S., Kallipolitou, A., Woehlke, G., Schliwa, M., & Meyhöfer, E. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74991-1 · Cited by 44
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Sellers, J. R., & Knight, P. J. (2007) · Journal of Muscle Research and Cell Motility · doi:10.1007/s10974-008-9134-0 · Cited by 44
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Vale, R. D. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90440-k · Cited by 44
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Jellali, A., Metz‐Boutigue, M., Surgucheva, I. G., Jancsik, V., Schwartz, C., Filliol, D., Gelfand, V. I., & Rendón, Á. (1994) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970280108 · Cited by 43

Authors: Hackney, D. D., Levitt, J. D., & Suhan, J.
Affiliations: Carnegie Mellon University (US)
ORCID: Hackney, D.D.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 1992-04
Volume: 267
Issue: 12
Pages: 8696-8701
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1016/s0021-9258(18)42499-4
OpenAlex: W1528749730
Cited by: 175
References: 31
Citations by year: 2026: 4 · 2025: 4 · 2024: 2 · 2023: 1 · 2022: 2 · 2020: 2 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 2 · 2015: 1 · 2014: 7 · 2013: 9 · 2012: 6
FWCI: 3.53
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 10419 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5r01ar025980-11)
National Institute of Neurological Disorders and Stroke (NS28562, R01NS028562)
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR25980)
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
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: kinesin, conformational change, ionic strength, sedimentation coefficient, diffusion coefficient, ATP binding, ADP, MgATP, protein folding
MeSH terms: Animals, Brain, Cattle, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Microscopy, Electron, Osmolar Concentration, Potassium Chloride, Protein Conformation, Sodium Chloride, Kinesins

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Kinesin undergoes a 9 S to 6 S conformational transition

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