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Vol. 18, Issue 7, 2503-2510, July 2007

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Protein Arms in the Kinetochore-Microtubule Interface of the Yeast DASH Complex

JJ L. Miranda^*,, David S. King, and Stephen C. Harrison

*Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138; Department of Molecular and Cell Biology, and Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; and Department of Biological Chemistry and Molecular Pharmacology, and Howard Hughes Medical Institute, Harvard Medical School, Boston, MA 02115

Submitted February 16, 2007; Revised April 10, 2007; Accepted April 17, 2007
Monitoring Editor: Kerry Bloom

The yeast DASH complex is a heterodecameric component of the kinetochore necessary for accurate chromosome segregation. DASH forms closed rings around microtubules with a large gap between the DASH ring and the microtubule cylinder. We characterized the microtubule-binding properties of limited proteolysis products and subcomplexes of DASH, thus identifying candidate polypeptide extensions involved in establishing the DASH-microtubule interface. The acidic C-terminal extensions of tubulin subunits are not essential for DASH binding. We also measured the molecular mass of DASH rings on microtubules with scanning transmission electron microscopy and found that approximately 25 DASH heterodecamers assemble to form each ring. Dynamic association and relocation of multiple flexible appendages of DASH may allow the kinetochore to translate along the microtubule surface.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

Present address: Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158.

Address correspondence to: Stephen C. Harrison (harrison{at}crystal.harvard.edu).

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