8QV0

Structure of the native microtubule lattice nucleated from the yeast spindle pole body

8QV0 の概要

• エントリーDOI: 10.2210/pdb8qv0/pdb
• EMDBエントリー: 18664
• 分子名称: Tubulin alpha-1 chain, Tubulin beta chain (2 entities in total)
• 機能のキーワード: microtubule nucleation, mtoc, y-tubulin, spb, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast); 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 1310677.21

構造登録者

Dendooven, T.,Yatskevich, S.,Burt, A.,Bellini, D.,Kilmartin, J.,Barford, D. (登録日: 2023-10-17, 公開日: 2024-04-24, 最終更新日: 2024-07-31)

主引用文献

Dendooven, T.,Yatskevich, S.,Burt, A.,Chen, Z.A.,Bellini, D.,Rappsilber, J.,Kilmartin, J.V.,Barford, D.
Structure of the native gamma-tubulin ring complex capping spindle microtubules.
Nat.Struct.Mol.Biol., 31:1134-1144, 2024

PubMed Abstract: Microtubule (MT) filaments, composed of α/β-tubulin dimers, are fundamental to cellular architecture, function and organismal development. They are nucleated from MT organizing centers by the evolutionarily conserved γ-tubulin ring complex (γTuRC). However, the molecular mechanism of nucleation remains elusive. Here we used cryo-electron tomography to determine the structure of the native γTuRC capping the minus end of a MT in the context of enriched budding yeast spindles. In our structure, γTuRC presents a ring of γ-tubulin subunits to seed nucleation of exclusively 13-protofilament MTs, adopting an active closed conformation to function as a perfect geometric template for MT nucleation. Our cryo-electron tomography reconstruction revealed that a coiled-coil protein staples the first row of α/β-tubulin of the MT to alternating positions along the γ-tubulin ring of γTuRC. This positioning of α/β-tubulin onto γTuRC suggests a role for the coiled-coil protein in augmenting γTuRC-mediated MT nucleation. Based on our results, we describe a molecular model for budding yeast γTuRC activation and MT nucleation.

PubMed: 38609662
DOI: 10.1038/s41594-024-01281-y

実験手法

ELECTRON MICROSCOPY (6.6 Å)