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A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility.

Publication ,  Journal Article
Thiede, C; Lakämper, S; Wessel, AD; Kramer, S; Schmidt, CF
Published in: Biophysical journal
January 2013

Homotetrameric kinesin-5 motors are essential for chromosome separation and assembly of the mitotic spindle. These kinesins bind between two microtubules (MTs) and slide them apart, toward the spindle poles. This process must be tightly regulated in mitosis. In in vitro assays, Eg5 moves diffusively on single MTs and switches to a directed mode between MTs. How allosteric communication between opposing motor domains works remains unclear, but kinesin-5 tail domains may be involved. Here we present a single-molecule fluorescence study of a tetrameric kinesin-1 head/kinesin-5 tail chimera, DK4mer. This motor exhibited fast processive motility on single MTs interrupted by pauses. Like Eg5, DK4mer diffused along MTs with ADP, and slid antiparallel MTs apart with ATP. In contrast to Eg5, diffusive and processive periods were clearly distinguishable. This allowed us to measure transition rates among states and for unbinding as a function of buffer ionic strength. These data, together with results from controls using tail-less dimers, indicate that there are two modes of interaction with MTs, separated by an energy barrier. This result suggests a scheme of motor regulation that involves switching between two bound states, possibly allosterically controlled by the opposing tetramer end. Such a scheme is likely to be relevant for the regulation of native kinesin-5 motors.

Duke Scholars

Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

January 2013

Volume

104

Issue

2

Start / End Page

432 / 441

Related Subject Headings

  • Xenopus Proteins
  • Saccharomyces cerevisiae
  • Recombinant Proteins
  • Protein Multimerization
  • Osmolar Concentration
  • Mutant Proteins
  • Molecular Sequence Data
  • Microtubules
  • Kinesins
  • Green Fluorescent Proteins
 

Citation

APA
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ICMJE
MLA
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Thiede, C., Lakämper, S., Wessel, A. D., Kramer, S., & Schmidt, C. F. (2013). A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility. Biophysical Journal, 104(2), 432–441. https://doi.org/10.1016/j.bpj.2012.11.3810
Thiede, Christina, Stefan Lakämper, Alok D. Wessel, Stefanie Kramer, and Christoph F. Schmidt. “A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility.Biophysical Journal 104, no. 2 (January 2013): 432–41. https://doi.org/10.1016/j.bpj.2012.11.3810.
Thiede C, Lakämper S, Wessel AD, Kramer S, Schmidt CF. A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility. Biophysical journal. 2013 Jan;104(2):432–41.
Thiede, Christina, et al. “A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility.Biophysical Journal, vol. 104, no. 2, Jan. 2013, pp. 432–41. Epmc, doi:10.1016/j.bpj.2012.11.3810.
Thiede C, Lakämper S, Wessel AD, Kramer S, Schmidt CF. A chimeric kinesin-1 head/kinesin-5 tail motor switches between diffusive and processive motility. Biophysical journal. 2013 Jan;104(2):432–441.
Journal cover image

Published In

Biophysical journal

DOI

EISSN

1542-0086

ISSN

0006-3495

Publication Date

January 2013

Volume

104

Issue

2

Start / End Page

432 / 441

Related Subject Headings

  • Xenopus Proteins
  • Saccharomyces cerevisiae
  • Recombinant Proteins
  • Protein Multimerization
  • Osmolar Concentration
  • Mutant Proteins
  • Molecular Sequence Data
  • Microtubules
  • Kinesins
  • Green Fluorescent Proteins