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Vol. 14, Issue 11, 4557-4568, November 2003

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Binding of the Essential Saccharomyces cerevisiae Kinetochore Protein Ndc10p to CDEII

Christopher W. Espelin ^* , Kim T. Simons ^*  , Stephen C. Harrison , and Peter K. Sorger ^* 

^* Department of Biology, Massachusetts Institute of Technology, Cambridge Massachusetts 02139; Departments of Biological Chemistry and Molecular Pharmacology and Pediatrics (HMS), Harvard University, Howard Hughes Medical Institute, Laboratory of Molecular Medicine, Enders Research Building, Children's Hospital, Boston, Massachusetts 02115

Submitted August 26, 2002; Revised June 24, 2003; Accepted July 15, 2003
Monitoring Editor: Tim Stearns

Chromosome segregation at mitosis depends critically on the accurate assembly of kinetochores and their stable attachment to microtubules. Analysis of Saccharomyces cerevisiae kinetochores has shown that they are complex structures containing 50 protein components. Many of these yeast proteins have orthologs in animal cells, suggesting that key aspects of kinetochore structure have been conserved through evolution, despite the remarkable differences between the 125-base pair 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.

Corresponding author. E-mail address: psorger{at}mit.edu.

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