9D0T

Proteasome core particle assembly intermediate Blm10:13S purified from Saccharomyces cerevisiae

9D0T の概要

• エントリーDOI: 10.2210/pdb9d0t/pdb
• EMDBエントリー: 46461
• 分子名称: Proteasome subunit alpha type-1, Proteasome subunit beta type-4, Proteasome activator BLM10, ... (12 entities in total)
• 機能のキーワード: proteasome, assembly chaperone, blm10, pa200, blm10-13s, pba1, cp, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 540819.58

構造登録者

Chen, X.,Kaur, M.,Roelofs, J.,Walters, K.J. (登録日: 2024-08-07, 公開日: 2024-12-04, 最終更新日: 2026-03-04)

主引用文献

Kaur, M.,Chen, X.,Lee, S.Y.,Weaver, T.M.,Freudenthal, B.D.,Walters, K.J.,Roelofs, J.
Structure of Blm10:13S proteasome intermediate reveals parallel assembly pathways for the proteasome core particle.
Biorxiv, 2024

PubMed Abstract: Proteasomes are formed by chaperone-assisted assembly of core particles (CPs) and regulatory particles (RPs). The CP chaperone dimer Pba1/Pba2 binds early to proteasome subunits, and is thought to be replaced by Blm10 to form Blm10:CP, which promotes ATP-independent degradation of disordered proteins. Here, we present evidence of distinct parallel assembly pathways for CP by solving five cryo-EM structures including a Blm10:13S pre-assembly intermediate. Our data conflict with the current model of Blm10 and Pba1/Pba2 sequential activity in a single assembly pathway, as we find their CP binding is mutually exclusive and both are present on early and late assembly intermediates. CP affinity for Pba1/Pba2 is reduced during maturation, promoting Pba1/Pba2 release. We find Blm10 undergoes no such affinity switch, suggesting this pathway predominantly yields mature Blm10-bound CP. Altogether, our findings conflict with the current paradigm of sequential CP binding to instead indicate parallel assembly pathways by Pba1/Pba2 and Blm10.

PubMed: 39574619
DOI: 10.1101/2024.11.04.621988

実験手法

ELECTRON MICROSCOPY (2.84 Å)