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TitleCM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation.
Journal, issue, pagesElife, Vol. 10, Year 2021
Publish dateMay 5, 2021
AuthorsAxel F Brilot / Andrew S Lyon / Alex Zelter / Shruthi Viswanath / Alison Maxwell / Michael J MacCoss / Eric G Muller / Andrej Sali / Trisha N Davis / David A Agard /
PubMed AbstractMicrotubule (MT) nucleation is regulated by the γ-tubulin ring complex (γTuRC), conserved from yeast to humans. In , γTuRC is composed of seven identical γ-tubulin small complex (γTuSC) sub- ...Microtubule (MT) nucleation is regulated by the γ-tubulin ring complex (γTuRC), conserved from yeast to humans. In , γTuRC is composed of seven identical γ-tubulin small complex (γTuSC) sub-assemblies, which associate helically to template MT growth. γTuRC assembly provides a key point of regulation for the MT cytoskeleton. Here, we combine crosslinking mass spectrometry, X-ray crystallography, and cryo-EM structures of both monomeric and dimeric γTuSCs, and open and closed helical γTuRC assemblies in complex with Spc110p to elucidate the mechanisms of γTuRC assembly. γTuRC assembly is substantially aided by the evolutionarily conserved CM1 motif in Spc110p spanning a pair of adjacent γTuSCs. By providing the highest resolution and most complete views of any γTuSC assembly, our structures allow phosphorylation sites to be mapped, surprisingly suggesting that they are mostly inhibitory. A comparison of our structures with the CM1 binding site in the human γTuRC structure at the interface between GCP2 and GCP6 allows for the interpretation of significant structural changes arising from CM1 helix binding to metazoan γTuRC.
External linksElife / PubMed:33949948 / PubMed Central
MethodsEM (helical sym.) / EM (single particle) / X-ray diffraction
Resolution2.00001856449 - 4.45 Å
Structure data

EMDB-23635, PDB-7m2w:
Engineered disulfide cross-linked closed conformation of the Yeast gamma-TuRC(SS)
Method: EM (helical sym.) / Resolution: 3 Å

EMDB-23636, PDB-7m2x:
Open conformation of the Yeast wild-type gamma-TuRC
Method: EM (helical sym.) / Resolution: 3.6 Å

EMDB-23637, PDB-7m2y:
Closed conformation of the Yeast wild-type gamma-TuRC
Method: EM (helical sym.) / Resolution: 4.03 Å

EMDB-23638, PDB-7m2z:
Monomeric single-particle reconstruction of the Yeast gamma-TuSC
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-23639:
Single-particle reconstruction of a dimer of the Yeast gamma-TuSC
Method: EM (single particle) / Resolution: 4.45 Å

PDB-7m3p:
Xrcc4-Spc110p(164-207) fusion
Method: X-RAY DIFFRACTION / Resolution: 2.00001856449 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

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

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (baker's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • homo sapiens (human)
KeywordsCELL CYCLE / microtubule nucleation

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