Letter abstract


Nature Cell Biology 5, 1079 - 1082 (2003)
Published online: 23 November 2003 | doi:10.1038/ncb1067

Alternate fast and slow stepping of a heterodimeric kinesin molecule

Kuniyoshi Kaseda1,2, Hideo Higuchi3 & Keiko Hirose1

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A conventional kinesin molecule travels continuously along a microtubule in discrete 8-nm steps. This processive movement is generally explained by models in which the two identical heads of a kinesin move in a 'hand-over-hand' manner1, 2, 3, 4. Here, we show that a single heterodimeric kinesin molecule (in which one of the two heads is mutated in a nucleotide-binding site) exhibits fast and slow (with the dwell time at least 10 times longer than that of the fast step) 8-nm steps alternately, presumably corresponding to the displacement by the wild-type and mutant heads, respectively. Our results provide the first direct evidence for models in which the roles of the two heads alternate every 8-nm step.

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  1. Gene Function Research Center, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba, Ibaraki 305-8562, Japan.
  2. Japan Society for the Promotion of Science (JSPS), 1-1-1 Higashi, Tsukuba, Ibaraki 305-8562, Japan.
  3. Department of Metallurgy, Graduate School of Engineering and Center for Interdisciplinary Research, Tohoku University, Sendai, Miyagi 980-8579, Japan.

Correspondence to: Keiko Hirose1 e-mail: k.hirose@aist.go.jp



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REFERENCE
Motor Proteins
Nature Encyclopaedia of Life Sciences

REVIEWS
WALKING ON TWO HEADS: THE MANY TALENTS OF KINESIN
Nature Reviews Molecular Cell Biology Review Article (01 Oct 2000)
 See all 2 matches for Reviews

NEWS AND VIEWS
Kinesin: walking or limping?
Nature Cell Biology News and Views (01 Dec 2003)
Kinesin–ADP: whole lotta shakin' goin' on
Nature Structural Biology News and Views (01 Jun 2001)

RESEARCH
Substeps within the 8-nm step of the ATPase cycle of single kinesin molecules
Nature Cell Biology Brief Communication (01 Apr 2001)
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