3UAI

Structure of the Shq1-Cbf5-Nop10-Gar1 complex from Saccharomyces cerevisiae

3UAI の概要

• エントリーDOI: 10.2210/pdb3uai/pdb
• 関連するPDBエントリー: 3UAH
• 分子名称: H/ACA ribonucleoprotein complex subunit 4, H/ACA ribonucleoprotein complex subunit 3, H/ACA ribonucleoprotein complex subunit 1, ... (4 entities in total)
• 機能のキーワード: h/aca rnp assembly intermediate, h/aca rna, nuclear, isomerase-chaperone complex, isomerase/chaperone
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Nucleus, nucleolus: P33322 Q6Q547 P28007; Nucleus: P40486
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 107178.02

構造登録者

Ye, K. (登録日: 2011-10-21, 公開日: 2011-12-14, 最終更新日: 2023-11-01)

主引用文献

Li, S.,Duan, J.,Li, D.,Ma, S.,Ye, K.
Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita
Embo J., 30:5010-5020, 2011

PubMed Abstract: Shq1 is a conserved protein required for the biogenesis of eukaryotic H/ACA ribonucleoproteins (RNPs), including human telomerase. We report the structure of the Shq1-specific domain alone and in complex with H/ACA RNP proteins Cbf5, Nop10 and Gar1. The Shq1-specific domain adopts a novel helical fold and primarily contacts the PUA domain and the otherwise disordered C-terminal extension (CTE) of Cbf5. The structure shows that dyskeratosis congenita mutations found in the CTE of human Cbf5 likely interfere with Shq1 binding. However, most mutations in the PUA domain are not located at the Shq1-binding surface and also have little effect on the yeast Cbf5-Shq1 interaction. Shq1 binds Cbf5 independently of the H/ACA RNP proteins Nop10, Gar1 and Nhp2 and the assembly factor Naf1, but shares an overlapping binding surface with H/ACA RNA. Shq1 point mutations that disrupt Cbf5 interaction suppress yeast growth particularly at elevated temperatures. Our results suggest that Shq1 functions as an assembly chaperone that protects the Cbf5 protein complexes from non-specific RNA binding and aggregation before assembly of H/ACA RNA.

PubMed: 22117216
DOI: 10.1038/emboj.2011.427

実験手法

X-RAY DIFFRACTION (3.06 Å)