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TitleThe cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5705, Year 2020
Publish dateNov 11, 2020
AuthorsErik Zupa / Anjun Zheng / Annett Neuner / Martin Würtz / Peng Liu / Anna Böhler / Elmar Schiebel / Stefan Pfeffer /
PubMed AbstractThe nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is ...The nucleation of microtubules from αβ-tubulin subunits is mediated by γ-tubulin complexes, which vary in composition across organisms. Aiming to understand how de novo microtubule formation is achieved and regulated by a minimal microtubule nucleation system, we here determined the cryo-electron microscopy structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution. Compared to the vertebrate γ-tubulin ring complex (γ-TuRC), we observed a vastly remodeled interface between the SPC/GCP-γ-tubulin spokes, which stabilizes the complex and defines the γ-tubulin arrangement. The relative positioning of γ-tubulin subunits indicates that a conformational rearrangement of the complex is required for microtubule nucleation activity, which follows opposing directionality as predicted for the vertebrate γ-TuRC. Collectively, our data suggest that the assembly and regulation mechanisms of γ-tubulin complexes fundamentally differ between the microtubule nucleation systems in lower and higher eukaryotes.
External linksNat Commun / PubMed:33177498 / PubMed Central
MethodsEM (single particle)
Resolution3.6 Å
Structure data

11835

7anz

EMDB-11835, PDB-7anz:
Structure of the Candida albicans gamma-Tubulin Small Complex
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • candida albicans (yeast)
KeywordsCYTOSOLIC PROTEIN / gamma-Tubulin Small Complex / Cytoskeleton / Microtubule nucleation

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