Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 282, Issue 9, Pages 6356-6363Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M609658200
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Funding
- NIGMS NIH HHS [R01 GM055440-09A1, R01 GM029169, R37 GM029169-24, R01 GM029169-29, R37 GM029169-23, GM55440, R37 GM029169, R01 GM055440, R01 GM067624, R37 GM29169, GM 67624, R01 GM055440-08] Funding Source: Medline
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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, transfermessenger RNA, and small protein Bs but in the absence of SI. 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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