+検索条件
-Structure paper
タイトル | Structural Basis for Bacterial Ribosome-Associated Quality Control by RqcH and RqcP. |
---|---|
ジャーナル・号・ページ | Mol Cell, Vol. 81, Issue 1, Page 115-126.e7, Year 2021 |
掲載日 | 2021年1月7日 |
著者 | Caillan Crowe-McAuliffe / Hiraku Takada / Victoriia Murina / Christine Polte / Sergo Kasvandik / Tanel Tenson / Zoya Ignatova / Gemma C Atkinson / Daniel N Wilson / Vasili Hauryliuk / |
PubMed 要旨 | In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, ...In all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality control (RQC) pathways. RQC begins with the splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal "tails." How such tailing can occur without the regular suite of translational components is, however, unclear. Using single-particle cryo-electron microscopy (EM) of native complexes, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with RqcP, an Hsp15 family protein. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit. |
リンク | Mol Cell / PubMed:33259810 |
手法 | EM (単粒子) |
解像度 | 2.6 - 4.9 Å |
構造データ | EMDB-11889, PDB-7as8: EMDB-11890, PDB-7as9: EMDB-11891, PDB-7asa: EMDB-11913: EMDB-11914: EMDB-11915: EMDB-11916: EMDB-11917: EMDB-11918: EMDB-11919: EMDB-11920: |
由来 |
|
キーワード | TRANSLATION / 50S / tRNA / RQC / RqcH / peptidyl-tRNA / RqcP / YabO / alanine tailing |