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- Title
Alternate fast and slow stepping of a heterodimeric kinesin molecule.
- Authors
Kaseda, Kuniyoshi; Higuchi, Hideo; Hirose, Keiko
- Abstract
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' manner. 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.
- Subjects
KINESIN; MICROTUBULES; EVIDENCE; RESEARCH; HAND
- Publication
Nature Cell Biology, 2003, Vol 5, Issue 12, p1079
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb1067