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TitleKar3Vik1, a member of the kinesin-14 superfamily, shows a novel kinesin microtubule binding pattern.
Journal, issue, pagesJ Cell Biol, Vol. 197, Issue 7, Page 957-970, Year 2012
Publish dateJun 25, 2012
AuthorsKatherine C Rank / Chun Ju Chen / Julia Cope / Ken Porche / Andreas Hoenger / Susan P Gilbert / Ivan Rayment /
PubMed AbstractKinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the ...Kinesin-14 motors generate microtubule minus-end-directed force used in mitosis and meiosis. These motors are dimeric and operate with a nonprocessive powerstroke mechanism, but the role of the second head in motility has been unclear. In Saccharomyces cerevisiae, the Kinesin-14 Kar3 forms a heterodimer with either Vik1 or Cik1. Vik1 contains a motor homology domain that retains microtubule binding properties but lacks a nucleotide binding site. In this case, both heads are implicated in motility. Here, we show through structural determination of a C-terminal heterodimeric Kar3Vik1, electron microscopy, equilibrium binding, and motility that at the start of the cycle, Kar3Vik1 binds to or occludes two αβ-tubulin subunits on adjacent protofilaments. The cycle begins as Vik1 collides with the microtubule followed by Kar3 microtubule association and ADP release, thereby destabilizing the Vik1-microtubule interaction and positioning the motor for the start of the powerstroke. The results indicate that head-head communication is mediated through the adjoining coiled coil.
External linksJ Cell Biol / PubMed:22734002 / PubMed Central
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-4etp:
C-terminal motor and motor homology domain of Kar3Vik1 fused to a synthetic heterodimeric coiled coil
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-EBC:
N,N'-ethane-1,2-diylbis(2-iodoacetamide)

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMOTOR PROTEIN / Kinesin Motor Protein / Kinesin Motor Homology Domain / karyogamy / mitosis / microtubules / internal Vik1 crosslink with N / N-Ethylenebis(iodoacetamide) / Nucleus

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