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-Structure paper
タイトル | RAPP-containing arrest peptides induce translational stalling by short circuiting the ribosomal peptidyltransferase activity. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 2432, Year 2024 |
掲載日 | 2024年3月19日 |
著者 | Martino Morici / Sara Gabrielli / Keigo Fujiwara / Helge Paternoga / Bertrand Beckert / Lars V Bock / Shinobu Chiba / Daniel N Wilson / |
PubMed 要旨 | Arrest peptides containing RAPP (ArgAlaProPro) motifs have been discovered in both Gram-positive and Gram-negative bacteria, where they are thought to regulate expression of important protein ...Arrest peptides containing RAPP (ArgAlaProPro) motifs have been discovered in both Gram-positive and Gram-negative bacteria, where they are thought to regulate expression of important protein localization machinery components. Here we determine cryo-EM structures of ribosomes stalled on RAPP arrest motifs in both Bacillus subtilis and Escherichia coli. Together with molecular dynamics simulations, our structures reveal that the RAPP motifs allow full accommodation of the A-site tRNA, but prevent the subsequent peptide bond from forming. Our data support a model where the RAP in the P-site interacts and stabilizes a single hydrogen atom on the Pro-tRNA in the A-site, thereby preventing an optimal geometry for the nucleophilic attack required for peptide bond formation to occur. This mechanism to short circuit the ribosomal peptidyltransferase activity is likely to operate for the majority of other RAPP-like arrest peptides found across diverse bacterial phylogenies. |
リンク | Nat Commun / PubMed:38503735 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.2 - 2.9 Å |
構造データ | EMDB-18320, PDB-8qbt: EMDB-18332, PDB-8qcq: EMDB-18340: ApdP-SRC with P-tRNA only EMDB-18341: ApdA-SRC with P-tRNA only |
化合物 | ChemComp-MG: ChemComp-K: ChemComp-PRO: ChemComp-ZN: ChemComp-HOH: |
由来 |
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キーワード | RIBOSOME (リボソーム) / Stalling / nascent chain / translation arrest / regulation (規制) / elongation arrest |