4ZN4

Crystal structure of Sqt1 from Chaetomium thermophilum solved by MR

4ZN4 の概要

• エントリーDOI: 10.2210/pdb4zn4/pdb
• 関連するPDBエントリー: 4ZOV 4ZOX 4ZOY 4ZOZ
• 分子名称: sqt1, GLYCEROL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: ribosome biogenesis, chaperone
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114347.26

構造登録者

Ahmed, Y.L.,Sinning, I. (登録日: 2015-05-04, 公開日: 2015-07-01, 最終更新日: 2024-01-10)

主引用文献

Pausch, P.,Singh, U.,Ahmed, Y.L.,Pillet, B.,Murat, G.,Altegoer, F.,Stier, G.,Thoms, M.,Hurt, E.,Sinning, I.,Bange, G.,Kressler, D.
Co-translational capturing of nascent ribosomal proteins by their dedicated chaperones.
Nat Commun, 6:7494-7494, 2015

PubMed Abstract: Exponentially growing yeast cells produce every minute >160,000 ribosomal proteins. Owing to their difficult physicochemical properties, the synthesis of assembly-competent ribosomal proteins represents a major challenge. Recent evidence highlights that dedicated chaperone proteins recognize the N-terminal regions of ribosomal proteins and promote their soluble expression and delivery to the assembly site. Here we explore the intuitive possibility that ribosomal proteins are captured by dedicated chaperones in a co-translational manner. Affinity purification of four chaperones (Rrb1, Syo1, Sqt1 and Yar1) selectively enriched the mRNAs encoding their specific ribosomal protein clients (Rpl3, Rpl5, Rpl10 and Rps3). X-ray crystallography reveals how the N-terminal, rRNA-binding residues of Rpl10 are shielded by Sqt1's WD-repeat β-propeller, providing mechanistic insight into the incorporation of Rpl10 into pre-60S subunits. Co-translational capturing of nascent ribosomal proteins by dedicated chaperones constitutes an elegant mechanism to prevent unspecific interactions and aggregation of ribosomal proteins on their road to incorporation.

PubMed: 26112308
DOI: 10.1038/ncomms8494

実験手法

X-RAY DIFFRACTION (1.94 Å)