Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0047148
Title: Altered Nucleotide-Microtubule Coupling and Increased Mechanical Output by a Kinesin Mutant
Authors: Liu H.-L.
Hallen M.A.
Endow S.A. 
Keywords: adenosine diphosphate
adenosine triphosphate
kinesin
nucleotide
amino acid sequence
animal cell
article
beta sheet
binding affinity
cell structure
controlled study
Drosophila
enzyme active site
hydrolysis
microtubule
microtubule assembly
molecular mechanics
mutant
nonhuman
wild type
Adenosine Triphosphate
Animals
Catalytic Domain
Drosophila
Drosophila Proteins
Kinesin
Microtubules
Models, Molecular
Nucleotides
Point Mutation
Protein Binding
Protein Structure, Secondary
Issue Date: 2012
Citation: Liu H.-L., Hallen M.A., Endow S.A. (2012). Altered Nucleotide-Microtubule Coupling and Increased Mechanical Output by a Kinesin Mutant. PLoS ONE 7 (10) : e47148. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0047148
Abstract: Kinesin motors hydrolyze ATP to produce force and do work in the cell - how the motors do this is not fully understood, but is thought to depend on the coupling of ATP hydrolysis to microtubule binding by the motor. Transmittal of conformational changes from the microtubule- to the nucleotide-binding site has been proposed to involve the central ?-sheet, which could undergo large structural changes important for force production. We show here that mutation of an invariant residue in loop L7 of the central ?-sheet of the Drosophila kinesin-14 Ncd motor alters both nucleotide and microtubule binding, although the mutated residue is not present in either site. Mutants show weak-ADP/tight-microtubule binding, instead of tight-ADP/weak-microtubule binding like wild type - they hydrolyze ATP faster than wild type, move faster in motility assays, and assemble long spindles with greatly elongated poles, which are also produced by simulations of assembly with tighter microtubule binding and faster sliding. The mutated residue acts like a mechanochemical coupling element - it transmits changes between the microtubule-binding and active sites, and can switch the state of the motor, increasing mechanical output by the motor. One possibility, based on our findings, is that movements by the residue and the loop that contains it could bend or distort the central ?-sheet, mediating free energy changes that lead to force production. © 2012 Liu et al.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161718
ISSN: 19326203
DOI: 10.1371/journal.pone.0047148
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