How a circularized tmRNA moves through the ribosome

During trans-translation, transfer-messenger RNA (tmRNA) and small protein B (SmpB) together rescue ribosomes stalled on a truncated mRNA and tag the nascent polypeptide for degradation. We used cryo-electron microscopy to determine the structures of three key states of the tmRNA-SmpB-ribosome compl...

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Bibliographic Details
Published in:	Science (American Association for the Advancement of Science) Vol. 363; no. 6428; pp. 740 - 744
Main Authors:	Rae, Christopher D, Gordiyenko, Yuliya, Ramakrishnan, V
Format:	Journal Article
Language:	English
Published:	United States The American Association for the Advancement of Science 15-02-2019
Subjects:	Biodegradation Circularity Cryoelectron Microscopy Degradation Electron microscopy Escherichia coli Intermediates Motion mRNA Polypeptides Protein B Protein Biosynthesis Proteins Ribonucleic acid Ribosomes Ribosomes - chemistry RNA RNA, Bacterial - chemistry RNA-Binding Proteins - chemistry Thermus thermophilus TmRNA Translation
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Summary:	During trans-translation, transfer-messenger RNA (tmRNA) and small protein B (SmpB) together rescue ribosomes stalled on a truncated mRNA and tag the nascent polypeptide for degradation. We used cryo-electron microscopy to determine the structures of three key states of the tmRNA-SmpB-ribosome complex during trans translation at resolutions of 3.7 to 4.4 angstroms. The results show how tmRNA and SmpB act specifically on stalled ribosomes and how the circularized complex moves through the ribosome, enabling translation to switch from the old defective message to the reading frame on tmRNA.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0036-8075 1095-9203
DOI:	10.1126/science.aav9370