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Published 27 October 2003. doi:10.1083/jcb.200305100
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© The Rockefeller University Press, 0021-9525/2003/10/215 $8.00
The Journal of Cell Biology, Volume 163, Number 2, 215-222

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Architecture of the budding yeast kinetochore reveals a conserved molecular core



Stefan Westermann1, Iain M. Cheeseman1, Scott Anderson2, John R. Yates, III2, David G. Drubin1 and Georjana Barnes1

1 Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720
2 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037

Address correspondence to Georjana Barnes, Department of Molecular and Cell Biology, Barker Hall, University of California, Berkeley, Berkeley, CA 94720. Tel.: (510) 642-5962. Fax: (510) 643-0062. email: gbarnes{at}socrates.berkeley.edu

How kinetochore proteins are organized to connect chromosomes to spindle microtubules, and whether any structural and organizational themes are common to kinetochores from distantly related organisms, are key unanswered questions. Here, we used affinity chromatography and mass spectrometry to generate a map of kinetochore protein interactions. The budding yeast CENP-C homologue Mif2p specifically copurified with histones H2A, H2B, and H4, and with the histone H3-like CENP-A homologue Cse4p, strongly suggesting that Cse4p replaces histone H3 in a specialized centromeric nucleosome. A novel four-protein Mtw1 complex, the Nnf1p subunit of which has homology to the vertebrate kinetochore protein CENP-H, also copurified with Mif2p and a variety of central kinetochore proteins. We show that Mif2 is a critical in vivo target of the Aurora kinase Ipl1p. Chromatin immunoprecipitation studies demonstrated the biological relevance of these associations. We propose that a molecular core consisting of CENP-A, -C, -H, and Ndc80/HEC has been conserved from yeast to humans to link centromeres to spindle microtubules.

Key Words: microtubule; spindle; mitosis; nucleosome; Aurora kinase

The online version of this article contains supplemental material.

The present address of I.M. Cheeseman is Ludwig Institute for Cancer Research University of California, San Diego, La Jolla, CA 92093-0660.

Abbreviations used in this paper: ChIP, chromatin immunoprecipitation; MAST, motif alignment and search tool; TAP, tandem affinity purification.


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