Abstract:
: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.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Miranda JJ,King DS,Harrison SCdoi
10.1091/mbc.e07-02-0135subject
Has Abstractpub_date
2007-07-01 00:00:00pages
2503-10issue
7eissn
1059-1524issn
1939-4586pii
E07-02-0135journal_volume
18pub_type
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