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-Structure paper
タイトル | Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1. |
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ジャーナル・号・ページ | J Biol Chem, Vol. 282, Issue 9, Page 6356-6363, Year 2007 |
掲載日 | 2007年3月2日 |
著者 | Reynald Gillet / Sukhjit Kaur / Wen Li / Marc Hallier / Brice Felden / Joachim Frank / |
PubMed 要旨 | A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer- ...A eubacterial ribosome stalled on a defective mRNA can be released through a quality control mechanism referred to as trans-translation, which depends on the coordinating binding actions of transfer-messenger RNA, small protein B, and ribosome protein S1. By means of cryo-electron microscopy, we obtained a map of the complex composed of a stalled ribosome and small protein B, which appears near the decoding center. This result suggests that, when lacking a codon, the A-site on the small subunit is a target for small protein B. To investigate the role of S1 played in trans-translation, we obtained a cryo-electron microscopic map, including a stalled ribosome, transfer-messenger RNA, and small protein Bs but in the absence of S1. In this complex, several connections between the 30 S subunit and transfer-messenger RNA that appear in the +S1 complex are no longer found. We propose the unifying concept of scaffolding for the roles of small protein B and S1 in binding of transfer-messenger RNA to the ribosome during trans-translation, and we infer a pathway of sequential binding events in the initial phase of trans-translation. |
リンク | J Biol Chem / PubMed:17179154 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 11.8 - 13.6 Å |
構造データ | EMDB-1310: Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1. EMDB-1312: |
由来 |
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キーワード | RNA BINDING PROTEIN/RNA / tmRNA / SmpB / RNA BINDING PROTEIN-RNA COMPLEX |