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TitleAssembly of the asymmetric human γ-tubulin ring complex by RUVBL1-RUVBL2 AAA ATPase.
Journal, issue, pagesSci Adv, Vol. 6, Issue 51, Year 2020
Publish dateDec 18, 2020
AuthorsFabian Zimmermann / Marina Serna / Artur Ezquerra / Rafael Fernandez-Leiro / Oscar Llorca / Jens Luders /
PubMed AbstractThe microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has ...The microtubule nucleator γ-tubulin ring complex (γTuRC) is essential for the function of microtubule organizing centers such as the centrosome. Since its discovery over two decades ago, γTuRC has evaded in vitro reconstitution and thus detailed structure-function studies. Here, we show that a complex of RuvB-like protein 1 (RUVBL1) and RUVBL2 "RUVBL" controls assembly and composition of γTuRC in human cells. Likewise, RUVBL assembles γTuRC from a minimal set of core subunits in a heterologous coexpression system. RUVBL interacts with γTuRC subcomplexes but is not part of fully assembled γTuRC. Purified, reconstituted γTuRC has nucleation activity and resembles native γTuRC as revealed by its cryo-electron microscopy (cryo-EM) structure at ~4.0-Å resolution. We further use cryo-EM to identify features that determine the intricate, higher-order γTuRC architecture. Our work finds RUVBL as an assembly factor that regulates γTuRC in cells and allows production of recombinant γTuRC for future in-depth mechanistic studies.
External linksSci Adv / PubMed:33355144
MethodsEM (single particle)
Resolution4.13 Å
Structure data

11888

7as4

EMDB-11888, PDB-7as4:
Recombinant human gTuRC
Method: EM (single particle) / Resolution: 4.13 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

Source
  • homo sapiens (human)
KeywordsCELL CYCLE / microtubule organizing center / microtubule / gamma-tubulin ring complex / gamma-tubulin small complex / spindle organization / microtubule nucleation

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