The yeast DASH complex forms closed rings on microtubules

J. J L Miranda, Peter De Wulf, Peter K. Sorger, Stephen C. Harrison

Research output: Contribution to journalArticlepeer-review


The Saccharomyces cerevisiae DASH complex is an essential microtubule-binding component of the kinetochore. We coexpressed all ten subunits of this assembly in Escherichia coli and purified a single complex, a ∼210-kDa heterodecamer with an apparent stoichiometry of one copy of each subunit. The hydrodynamic properties of the recombinant assembly are indistinguishable from those of the native complex in yeast extracts. The structure of DASH alone and bound to microtubules was visualized by EM. The free heterodecamer is relatively globular. In the presence of microtubules, DASH oligomerizes to form rings and paired helices that encircle the microtubules. We discuss potential roles for such collar-like structures in maintaining microtubule attachment and spindle integrity during chromosome segregation.

Original languageEnglish
Pages (from-to)138-143
Number of pages6
JournalNature Structural and Molecular Biology
Issue number2
Publication statusPublished - Feb 20 2005

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


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