Proteomics

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Structure of the native gamma-Tubulin Ring Complex capping spindle microtubules


ABSTRACT: Microtubules (MTs) are fundamental to cellular architecture, function and organismal development. They are nucleated from microtubule organizing centres by the evolutionary conserved ?-tubulin ring complex (?TuRC). However, the molecular mechanism of nucleation remains elusive. Here, we used cryo-electron tomography (cryo-ET) to determine the structure of the native ?TuRC capping the minus end of a MT in the context of enriched budding yeast spindles. In our structure, ?TuRC presents a ring of ?-tubulin subunits to seed nucleation of exclusively 13-protofilament microtubules, and it adopts an active closed conformation to function as a perfect geometric template for MT nucleation. Our cryo-ET reconstruction also revealed that a novel coiled-coil protein staples the first row of ?/?-tubulin molecules to alternating positions along the ?-tubulin ring. This positioning of ?/?-tubulin onto ?TuRC suggests a role for the coiled-coil protein in augmenting ?TuRC-mediated microtubule nucleation. Based on our results we describe a molecular model for budding yeast ?TuRC activation and MT nucleation.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Catarina Franco  

LAB HEAD: David Barford

PROVIDER: PXD050372 | Pride | 2024-03-05

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
A1_F159389.dat Other
A2_F159403.dat Other
A3_F159420.dat Other
A4_F159436.dat Other
B1_F159390.dat Other
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