A plus-end-directed motor enzyme that moves antiparallel microtubules in vitro localizes to the interzone of mitotic spindles

Corey Nislow, Vivian A. Lombillo, Ryoko Kuriyama, J. Richard McIntosh

Research output: Contribution to journalArticlepeer-review

271 Scopus citations

Abstract

Mitosis comprises a complex set of overlapping motile events, many of which involve microtubule-dependent motor enzymes1,2. Here we describe a new member of the kinesin superfamily. The protein was originally identified as a spindle antigen by the CHO1 monoclonal antibody3 and shown to be required for mitotic progression4,5. We have cloned the gene that encodes this antigen and found that its sequence contains a domain with strong sequence similarity to the motor domain of kinesin-like proteins. The product of this gene, expressed in bacteria, can cross-bridge antiparallel microtubules in vitro, and in the presence of Mg-ATP, microtubules slide over one another in a fashion reminiscent of microtubule movements during spindle elongation.

Original languageEnglish (US)
Pages (from-to)543-547
Number of pages5
JournalNature
Volume359
Issue number6395
DOIs
StatePublished - Jan 1 1992

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