Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1.

Abstract : 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.
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Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (9), pp.6356-63. 〈10.1074/jbc.M609658200〉
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Dernière modification le : mercredi 16 mai 2018 - 11:23:16

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Reynald Gillet, Sukhjit Kaur, Wen Li, Marc Hallier, Brice Felden, et al.. Scaffolding as an organizing principle in trans-translation. The roles of small protein B and ribosomal protein S1.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2007, 282 (9), pp.6356-63. 〈10.1074/jbc.M609658200〉. 〈inserm-00712975〉

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