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Neck-linker length dependence of processive Kinesin-5 motility.

Publication ,  Journal Article
Düselder, A; Thiede, C; Schmidt, CF; Lakämper, S
Published in: Journal of molecular biology
October 2012

Processive motility of individual molecules is essential for the function of many kinesin motors. Processivity for kinesins relies on communication between the two heads of a dimeric molecule, such that binding strictly alternates. The main communicating elements are believed to be the two neck linkers connecting the motors' stalks and heads. A proposed mechanism for coordination is the transmission of stress through the neck linkers. It is believed that the efficiency of gating depends on the length of the neck linker. Recent studies have presented support for a simple model in which the length of the neck linker directly controls the degree of processivity. Based on a previously published Kinesin-1/Kinesin-5 chimera, Eg5Kin, we have analyzed the motility of 12 motor constructs: we have varied the length of the neck linker in the range between 9 and 21 amino acids using the corresponding native Kinesin-5 sequence (Xenopus laevis Eg5). We found, surprisingly, that neither velocity nor force generation depended on neck-linker length. We also found that constructs with short neck linkers, down to 12 amino acids, were still highly processive, while processivity was lost at a length of 9 amino acids. Run lengths were maximal with neck linkers close to the native Kinesin-5 length and decreased beyond that length. This finding generally confirms the coordinating role of the neck linker for kinesin motility but challenges the simplest model postulating a motor-type-independent optimal length. Instead, our results suggest that different kinesins might be optimized for different neck-linker lengths.

Duke Scholars

Published In

Journal of molecular biology

DOI

EISSN

1089-8638

ISSN

0022-2836

Publication Date

October 2012

Volume

423

Issue

2

Start / End Page

159 / 168

Related Subject Headings

  • Xenopus Proteins
  • Protein Conformation
  • Molecular Sequence Data
  • Microtubules
  • Kinesins
  • Biochemistry & Molecular Biology
  • Animals
  • Amino Acid Sequence
  • 3107 Microbiology
  • 3101 Biochemistry and cell biology
 

Citation

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Düselder, A., Thiede, C., Schmidt, C. F., & Lakämper, S. (2012). Neck-linker length dependence of processive Kinesin-5 motility. Journal of Molecular Biology, 423(2), 159–168. https://doi.org/10.1016/j.jmb.2012.06.043
Düselder, André, Christina Thiede, Christoph F. Schmidt, and Stefan Lakämper. “Neck-linker length dependence of processive Kinesin-5 motility.Journal of Molecular Biology 423, no. 2 (October 2012): 159–68. https://doi.org/10.1016/j.jmb.2012.06.043.
Düselder A, Thiede C, Schmidt CF, Lakämper S. Neck-linker length dependence of processive Kinesin-5 motility. Journal of molecular biology. 2012 Oct;423(2):159–68.
Düselder, André, et al. “Neck-linker length dependence of processive Kinesin-5 motility.Journal of Molecular Biology, vol. 423, no. 2, Oct. 2012, pp. 159–68. Epmc, doi:10.1016/j.jmb.2012.06.043.
Düselder A, Thiede C, Schmidt CF, Lakämper S. Neck-linker length dependence of processive Kinesin-5 motility. Journal of molecular biology. 2012 Oct;423(2):159–168.
Journal cover image

Published In

Journal of molecular biology

DOI

EISSN

1089-8638

ISSN

0022-2836

Publication Date

October 2012

Volume

423

Issue

2

Start / End Page

159 / 168

Related Subject Headings

  • Xenopus Proteins
  • Protein Conformation
  • Molecular Sequence Data
  • Microtubules
  • Kinesins
  • Biochemistry & Molecular Biology
  • Animals
  • Amino Acid Sequence
  • 3107 Microbiology
  • 3101 Biochemistry and cell biology