Article abstract
Nature Structural & Molecular Biology 14, 721 - 726 (2007)
Published online: 22 July 2007 | doi:10.1038/nsmb1274
Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms
Hong-Wei Wang1, Vincent H Ramey1,2, Stefan Westermann2,4, Andres E Leschziner2, Julie P I Welburn1, Yuko Nakajima2, David G Drubin2, Georjana Barnes2 & Eva Nogales1,2,3
Abstract
The Dam1 kinetochore complex is essential for chromosome segregation in budding yeast. This ten-protein complex self-assembles around microtubules, forming ring-like structures that move with depolymerizing microtubule ends, a mechanism with implications for cellular function. Here we used EM-based single-particle and helical analyses to define the architecture of the Dam1 complex at 30-Å resolution and the self-assembly mechanism. Ring oligomerization seems to be facilitated by a conformational change upon binding to microtubules, suggesting that the Dam1 ring is not preformed, but self-assembles around kinetochore microtubules. The C terminus of the Dam1p protein, where most of the Aurora kinase Ipl1 phosphorylation sites reside, is in a strategic location to affect oligomerization and interactions with the microtubule. One of Ipl1's roles might be to fine-tune the coupling of the microtubule interaction with the conformational change required for oligomerization, with phosphorylation resulting in ring breakdown.
- Life Sciences Division, Lawrence Berkeley National Laboratory, 1 Cyclotron Rd., Berkeley, California 94720, USA.
- Department of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
- Howard Hughes Medical Institute, University of California, Berkeley, California 94720, USA.
- Present address: Research Institute of Molecular Pathology, Dr. Bohr-Gasse 7, Vienna, Austria.
Correspondence to: Eva Nogales1,2,3 e-mail: enogales@lbl.gov
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