The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Kinesin undergoes a 9 S to 6 S conformational transition
Open accessAbstract
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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In the citing paper
“At physiological salt concentrations, purified kinesin is in a folded conformation in which the tail comes close to the motor domain, while, in high salt, kinesin is in an extended conformation.”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
In the citing paper
“Sedimentation in a high salt buffer (0.5 M NaCl) shifted the proteins to an extended 6S conformation at both pH 7.2 and 6.8 (Fig. 8 D), in agreement with the data obtained for purified kinesin (Hackney et al., 1992).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
In the citing paper
“At both pH values, the proteins sedimented at ∼9S (Fig. 8 D), corresponding to the folded conformation of kinesin in which the tail and motor domains are in proximity to each other (Hackney et al., 1992).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
In the citing paper
“Indeed, the sedimentation coefficient of 9S determined for kinesin in cell lysates corresponds to the folded conformation of purified kinesin as determined by sedimentation and electron microscopy analysis (Hirokawa et al., 1989; Hisanaga et al., 1989; Hackney et al., 1992).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Hackney et al., 1992
Citations
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Self-citation
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Metadata
- 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)
- 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
- 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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