JJ L Miranda1, Peter De Wulf2, Peter K Sorger2, 3
& Stephen C Harrison41
Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
2
Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
3
Biological Engineering Division, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
4
Department of Biological Chemistry and Molecular Pharmacology and Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Correspondence should be addressed to Stephen C Harrison harrison@crystal.harvard.edu
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.
