Cited by 194Microtubule and mitosis dynamicsForce Microscopy Techniques and ApplicationsProtein Structure and Dynamics

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Distinguishing Inchworm and Hand-Over-Hand Processive Kinesin Movement by Neck Rotation Measurements

Abstract

The motor enzyme kinesin makes hundreds of unidirectional 8-nanometer steps without detaching from or freely sliding along the microtubule on which it moves. We investigated the kinesin stepping mechanism by immobilizing a Drosophila kinesin derivative through the carboxyl-terminal end of the neck coiled-coil domain and measuring orientations of microtubules moved by single enzyme molecules at submicromolar adenosine triphosphate concentrations. The kinesin-mediated microtubule-surface linkage was sufficiently torsionally stiff (>/=2.0 +/- 0.9 x 10(-20) Newton meters per radian2) that stepping by the hypothesized symmetric hand-over-hand mechanism would produce 180 degree rotations of the microtubule relative to the immobilized kinesin neck. In fact, there were no rotations, a finding that is inconsistent with symmetric hand-over-hand movement. An alternative "inchworm" mechanism is consistent with our experimental results.

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Research works printed but not linked: 24

  1. 10.1146/annurev.cellbio.15.1.141 · DOI
  2. 10.1016/S0092-8674(00)80947-2 · DOI
  3. 10.1038/342154a0 · DOI · Paper page
  4. 10.1038/39247 · DOI
  5. 10.1016/0092-8674(94)90060-4 · DOI · Paper page
  6. 10.1016/S0092-8674(00)81562-7 · DOI
  7. 10.1126/science.283.5405.1152 · DOI · Paper page
  8. 10.1073/pnas.97.2.640 · DOI
  9. 10.1038/373718a0 · DOI
  10. 10.1083/jcb.140.6.1395 · DOI
  11. 10.1016/S0006-3495(01)75925-5 · DOI
  12. 10.1038/41111 · DOI · Paper page
  13. 10.1073/pnas.87.24.10053 · DOI · Paper page
  14. 10.1146/annurev.ph.58.030196.003415 · DOI
  15. 10.1038/23072 · DOI
  16. 10.1126/science.256.5055.350 · DOI
  17. Block S. M., Svoboda K., Biophys. J. 68, 2305S (1995).
  18. 10.1007/BF00122526 · DOI
  19. 10.1074/jbc.270.8.3926 · DOI
  20. 10.1016/S0021-9258(17)37238-1 · DOI
  21. 10.1073/pnas.90.24.11653 · DOI
  22. A. Hoenger et al. J. Mol. Biol. 297 1087 (2000). · DOI
  23. 10.1038/386299a0 · DOI
  24. A movie showing microtubule movement under this condition is available as supplementary material on Science Online at www.sciencemag.org/cgi/content/full/295/5556/844/DC1.

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Metadata

Authors
Hua, W., Chung, J., & Gelles, J.
Affiliations
  • Biophysics and Structural Biology Program,
  • Brandeis University (US)
Corresponding author
Gelles, Jeff
Venue
Science
Published
2002-02
Volume
295
Issue
5556
Pages
844-848
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1589896765
Cited by
194
References
0
Citations by year
2025: 3 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 3 · 2020: 4 · 2019: 4 · 2018: 5 · 2017: 4 · 2016: 7 · 2015: 3 · 2014: 10 · 2013: 4 · 2012: 14
FWCI
7.66
Type
journal article
Language
en
Open access
closed
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
kinesin, inchworm mechanism, hand-over-hand mechanism, torsional stiffness, microtubule sliding
MeSH terms
Adenosine Triphosphate, Adenylyl Imidodiphosphate, Animals, Binding Sites, Catalysis, Drosophila, Enzymes, Immobilized, Microtubules, Models, Biological, Movement, Rotation, Kinesins, Protein Structure, Tertiary, Dimerization, Streptavidin, Molecular Motor Proteins

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