Influence of the kinesin neck domain on dimerization and ATPase kinetics
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Motor domains of kinesin were expressed that extend from the N terminus to positions 346, 357, 365, 381, and 405 (designated DKH346-DKH405) to determine if the kinetic differences observed between monomeric DKH340 and dimeric DKH392 (Hackney, D. D. (1994) Proc. Natl. Acad. Sci. U. S. A. 91, 6865-6869) were specific to these constructs or due to their oligomeric state. Sedimentation analysis indicated that DKH346, DKH357, and DKH365 are predominantly monomeric and that DKH381 and DKH405 are predominantly dimeric at 0. 01-0.03 microM, the concentrations used for ATPase assays. In buffer with 25 mM KCl, all have high kcat values of 38-96 s-1 at saturating microtubule (MT) levels. Monomeric DKH346, DKH357, and DKH365 have K0.5(MT) values of 17, 9, and 1.4 microM, respectively, but the K0. 5(MT) values for the dimeric species are significantly lower, with 0. 02 and 0.14 microM for DKH381 and DKH405, respectively. The three new monomers release all of their ADP on association with microtubules, whereas the two new dimers retain approximately half of their ADP, consistent with the half-site reactivity observed previously with dimeric DKH392. Both the kbi(ATPase) (=kcat/K0. 5(MT)) values for stimulation of ATPase by MTs and the kbi(ADP) for stimulation of ADP release by MTs were determined in buffer containing 120 mM potassium acetate. The ratio of these rate constants (kbi(ratio) = kbi(ATPase)/kbi(ADP)) is 60-100 for the dimers, indicating hydrolysis of many ATP molecules per productive encounter with a MT as observed previously for DKH392 (Hackney, D. D. (1995) Nature 377, 448-450). For the monomers, kbi(ratio) values of approximately 4 indicate that they also may hydrolyze more than one ATP molecule per encounter with a MT and that the mechanism of hydrolysis is therefore fundamentally different from that of actomyosin. DKH340 is an exception to this pattern and may undergo uncoupled ATP hydrolysis.
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Members of the kinesin family of molecular motors are capable of taking over 100 steps on their microtubule track without dissociating.
“Members of the kinesin family of molecular motors are capable of taking over 100 steps on their microtubule track without dissociating”
From Stepping and Stretching (2003) · cites this paper as [4]
The introductory passage says native dimeric kinesin can move along a microtubule without net dissociation, and the Discussion describes highly processive movement. But the paper reports 60–100 ATP molecules hydrolyzed per productive microtubule encounter for the dimers; it does not establish that they take over 100 steps without dissociating. Page numbers are unavailable in our copy. (LLM, conf=0.87)
Experimental — accuracy not yet measuredThe apparent MT binding constant of HK420 in COS lysates agrees with the apparent binding constant for MTs based on activation of the ATPase activity of purified dimeric kinesin constructs.
“This value agrees with the apparent binding constant for MTs based on activation of the ATPase activity of purified dimeric kinesin constructs (Hackney, 1994, 1995; Rosenfeld et al., 1996; Jiang et al., 1997).”
From Light Chain– dependent Regulation of Kinesin's Interaction with Microtubules (1998) · cites this paper as Jiang et al., 1997
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Wada, Y., Hamasaki, T., & Satir, P. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.1.161 · Cited by 11 · see citing works
Properties of the Kinesin‐3 NcKin3 motor domain and implications for neck function
Adio, S., & Woehlke, G. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07083.x · Cited by 7 · see citing works
Computer Simulation of Assembly and Co-operativity of Hexameric AAA ATPases
Le, D. T.-V., Eckert, T., & Woehlke, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0067815 · Cited by 7 · see citing works
Walker, B. C., Tempel, W., Zhu, H., Park, H., & Cochran, J. C. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00011 · Cited by 6 · see citing works
Hackney, D., & McGoff, M. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.08.019 · Cited by 1 · see citing works
Self-citationBiased movement of monomeric kinesin-3 KLP-6 explained by a symmetric Brownian ratchet model
Kita, T., Sasaki, K., & Niwa, S. (2024) · Biophysical Journal · doi:10.1016/j.bpj.2024.11.3312 · Cited by 2 · see citing works
Motor proteins of the kinesin superfamily
Hackney, D. D. (2003) · The Enzymes · doi:10.1016/s1874-6047(04)80004-0 · Cited by 1 · see citing works
Self-citationKallipolitou, A. (2002) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.704
Crosslinking studies on the conventional kinesin of Neurospora crassa
Hahlen, K. (2004) · Elektronische Hochschulschriften der LMU München (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.2619
The Kinetic Characterization of the Marginally Processive Motor, Dimeric Eg5/KSP
Krzysiak, T. C. (2007) · D-Scholarship@Pitt (University of Pittsburgh)
Miyazono, Y., Hayashi, M., Karagiannis, P., Harada, Y., & Tadakuma, H. (2009)
Deavours, B. E. (2001) · VTechWorks (Virginia Tech)
Processivity of the monomeric KLP-6 kinesin and a Brownian ratchet model with symmetric potentialsPreprint
Kita, T., Sasaki, K., & Niwa, S. (2024) · bioRxiv · doi:10.1101/2024.08.06.606760 · Cited by 1 · see citing works
- Authors
- Jiang, W., Stock, M. F., Li, X., & Hackney, D. D.
- Affiliations
- Carnegie Mellon University (US)
- Corresponding author
- Hackney, David D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1997-03
- Volume
- 272
- Issue
- 12
- Pages
- 7626-7632
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2082002895
- Cited by
- 75
- References
- 33
- Citations by year
- 2024: 3 · 2019: 2 · 2016: 2 · 2015: 1 · 2013: 2
- FWCI
- 3.47
- 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
- National Cancer Institute
- National Institute of Neurological Disorders and Stroke (NS28562, R01NS028562)
- 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 › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- kinesin, ATPase kinetics, microtubule binding, half-site reactivity, ADP release, oligomeric state, kinesin motor protein, microtubule sliding
- MeSH terms
- Adenosine Diphosphate, Adenosine Triphosphatases, Biopolymers, Enzyme Activation, Kinetics, Microtubules, Kinesins
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