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- Title
Architecture of the Dam1 kinetochore ring complex and implications for microtubule-driven assembly and force-coupling mechanisms.
- Authors
Hong-Wei Wang; Ramey, Vincent H.; Westermann, Stefan; Leschziner, Andres E.; Welburn, Julie P. I.; Nakajima, Yuko; Drubin, David G.; Barnes, Georjana; Nogales, Eva
- 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.
- Publication
Nature Structural & Molecular Biology, 2007, Vol 14, Issue 8, p721
- ISSN
1545-9993
- Publication type
Academic Journal
- DOI
10.1038/nsmb1274