7OHY

Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL34 expression shut down, population B

これはPDB形式変換不可エントリーです。

7OHY の概要

• エントリーDOI: 10.2210/pdb7ohy/pdb
• EMDBエントリー: 12913
• 分子名称: 25S rRNA, 60S ribosomal protein L14-A, 60S ribosomal protein L15-A, ... (27 entities in total)
• 機能のキーワード: ribosomal assembly state, ribosome
• 由来する生物種: Saccharomyces cerevisiae S288C; 詳細
• タンパク質・核酸の鎖数: 26
• 化学式量合計: 1736478.31

構造登録者

Milkereit, P.,Poell, G. (登録日: 2021-05-11, 公開日: 2021-11-03, 最終更新日: 2024-07-10)

主引用文献

Poll, G.,Pilsl, M.,Griesenbeck, J.,Tschochner, H.,Milkereit, P.
Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors.
Plos One, 16:e0252497-e0252497, 2021

PubMed Abstract: In yeast and human cells many of the ribosomal proteins (r-proteins) are required for the stabilisation and productive processing of rRNA precursors. Functional coupling of r-protein assembly with the stabilisation and maturation of subunit precursors potentially promotes the production of ribosomes with defined composition. To further decipher mechanisms of such an intrinsic quality control pathway we analysed here the contribution of three yeast large ribosomal subunit r-proteins rpL2 (uL2), rpL25 (uL23) and rpL34 (eL34) for intermediate nuclear subunit folding steps. Structure models obtained from single particle cryo-electron microscopy analyses provided evidence for specific and hierarchic effects on the stable positioning and remodelling of large ribosomal subunit domains. Based on these structural and previous biochemical data we discuss possible mechanisms of r-protein dependent hierarchic domain arrangement and the resulting impact on the stability of misassembled subunits.

PubMed: 34813592
DOI: 10.1371/journal.pone.0252497

実験手法

ELECTRON MICROSCOPY (3.9 Å)