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Open Biol January 1, 2021; 11 (2): 200325.

Reconstitution of the recombinant human γ-tubulin ring complex.

Würtz M , Böhler A , Neuner A , Zupa E , Rohland L , Liu P , Vermeulen BJA , Pfeffer S , Eustermann S , Schiebel E .

Cryo-electron microscopy recently resolved the structure of the vertebrate γ-tubulin ring complex (γ-TuRC) purified from Xenopus laevis egg extract and human cells to near-atomic resolution. These studies clarified the arrangement and stoichiometry of γ-TuRC components and revealed that one molecule of actin and the small protein MZT1 are embedded into the complex. Based on this structural census of γ-TuRC core components, we developed a recombinant expression system for the reconstitution and purification of human γ-TuRC from insect cells. The recombinant γ-TuRC recapitulates the structure of purified native γ-TuRC and has similar functional properties in terms of microtubule nucleation and minus end capping. This recombinant system is a central step towards deciphering the activation mechanisms of the γ-TuRC and the function of individual γ-TuRC core components.

PubMed ID: 33529551
PMC ID: PMC8061689
Article link: Open Biol

Species referenced: Xenopus laevis
Genes referenced: actb golga4 myc tubgcp3 tubgcp5
GO keywords: gamma-tubulin ring complex

Article Images: [+] show captions
References [+] :
Aldaz, Insights into microtubule nucleation from the crystal structure of human gamma-tubulin. 2005, Pubmed