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A more recent version of this article appeared on November 1, 2003
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Submitted on August 26, 2002
Revised on June 24, 2003
Accepted on July 15, 2003
1 Massachusetts Institute of Technology, Dept of Biology, Room 68-371, 77 Massachusetts Avenue Cambridge Massachusetts 02139
2 Massachusetts Institute of Technology, Dept of Biology, Room 68-371, 77 Massachusetts Avenue Cambridge Massachusetts 02139, Harvard University, Departments of Biological Chemistry and Molecular Pharmacology and Pediatrics (HMS), Howard Hughes Medical Institute, Laboratory of Molecular Medicine, Enders Research Building, Children's Hospital, 320 Longwood Avenue, Boston, MA 02115
3 Harvard University, Departments of Biological Chemistry and Molecular Pharmacology and Pediatrics (HMS), Howard Hughes Medical Institute, Laboratory of Molecular Medicine, Enders Research Building, Children's Hospital, 320 Longwood Avenue, Boston, MA 02115
* Corresponding author. E-mail address: psorger{at}mit.edu.
Chromosome segregation at mitosis depends critically on the
accurate assembly of kinetochores and their stable
attachment to microtubules. Analysis of S. cerevisiae
kinetochores has shown that they are complex structures
containing 50 or more protein components. Many of these yeast proteins
have orthologues in animal cells, suggesting that key aspects of
kinetochore structure have been conserved through
evolution, despite the remarkable differences between the 125 base
pairs centromeres of budding yeast and the Mb centromeres of animal
cells. We describe here an analysis of S. cerevisiae
Ndc10p, one of the four protein components of the CBF3 complex. CBF3
binds to the CDEIII element of centromeric DNA and initiates
kinetochore assembly. Whereas CDEIII binding by Ndc10p
requires the other components of CBF3, Ndc10p can bind on its own to
CDEII, a region of centromeric DNA with no known binding partners.
Ndc10p-CDEII binding involves a dispersed set of sequence-selective and
nonselective contacts over 
80 base pairs of DNA, suggesting
formation of a multimeric structure. CDEII-like sites, active in Ndc10p
binding, are also present along chromosome arms. We propose that a
polymeric Ndc10p complex formed on CDEII and CDEIII DNA is the
foundation for recruiting microtubule attachment proteins to
kinetochores. A similar type of polymeric structure on
chromosome arms may mediate other chromosome-spindle interactions.
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