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- Title
Ring closure activates yeast γTuRC for species-specific microtubule nucleation.
- Authors
Kollman, Justin M; Greenberg, Charles H; Li, Sam; Moritz, Michelle; Zelter, Alex; Fong, Kimberly K; Fernandez, Jose-Jesus; Sali, Andrej; Kilmartin, John; Davis, Trisha N; Agard, David A
- Abstract
The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γγTuRC is assembled from repeating γγ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC structure showed γTuSC in an open conformation that prevents matching to microtubule symmetry. By contrast, we show here that γ-tubulin complexes are in a closed conformation when attached to microtubules. To confirm the functional importance of the closed γTuSC ring, we trapped the closed state and determined its structure, showing that the γ-tubulin ring precisely matches microtubule symmetry and providing detailed insight into γTuRC architecture. Importantly, the closed state is a stronger nucleator, thus suggesting that this conformational switch may allosterically control γTuRC activity. Finally, we demonstrate that γTuRCs have a strong preference for tubulin from the same species.
- Subjects
TUBULIN structure; RING formation (Chemistry); NUCLEATION; SACCHAROMYCES cerevisiae; MOLECULAR structure of oligomers; EUKARYOTIC evolution
- Publication
Nature Structural & Molecular Biology, 2015, Vol 22, Issue 2, p132
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.2953