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-Structure paper
タイトル | Structure of the Bacillus subtilis 70S ribosome reveals the basis for species-specific stalling. |
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ジャーナル・号・ページ | Nat Commun, Vol. 6, Page 6941, Year 2015 |
掲載日 | 2015年4月23日 |
著者 | Daniel Sohmen / Shinobu Chiba / Naomi Shimokawa-Chiba / C Axel Innis / Otto Berninghausen / Roland Beckmann / Koreaki Ito / Daniel N Wilson / |
PubMed 要旨 | Ribosomal stalling is used to regulate gene expression and can occur in a species-specific manner. Stalling during translation of the MifM leader peptide regulates expression of the downstream ...Ribosomal stalling is used to regulate gene expression and can occur in a species-specific manner. Stalling during translation of the MifM leader peptide regulates expression of the downstream membrane protein biogenesis factor YidC2 (YqjG) in Bacillus subtilis, but not in Escherichia coli. In the absence of structures of Gram-positive bacterial ribosomes, a molecular basis for species-specific stalling has remained unclear. Here we present the structure of a Gram-positive B. subtilis MifM-stalled 70S ribosome at 3.5-3.9 Å, revealing a network of interactions between MifM and the ribosomal tunnel, which stabilize a non-productive conformation of the PTC that prevents aminoacyl-tRNA accommodation and thereby induces translational arrest. Complementary genetic analyses identify a single amino acid within ribosomal protein L22 that dictates the species specificity of the stalling event. Such insights expand our understanding of how the synergism between the ribosome and the nascent chain is utilized to modulate the translatome in a species-specific manner. |
リンク | Nat Commun / PubMed:25903689 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.9 Å |
構造データ | |
由来 |
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キーワード | RIBOSOME (リボソーム) / stalling / translation arrest / mifm / L22 |