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tmRNA to the rescue: Structural motives for the salvage of stalled ribosomes
KTH, School of Technology and Health (STH), Structural Biotechnology (Closed 20130701).
2010 (English)In: RNA Biology, ISSN 1547-6286, Vol. 7, no 5, 577-581 p.Article in journal (Other academic) Published
Abstract [en]

During translation, mRNA molecules are incidentally damaged, leaving the ribosome unable to reach or recognize the stop codon and thus stalled with mRNA and a potentially harmful polypeptide product attached to tRNA in the ribosomal P-site. In bacteria, a process called trans-translation has evolved, where a protein-RNA complex (smpB-tmRNA) mimicks the role of aminoacyl charged tRNA in the ribosomal A-site. The ribosome then resumes protein synthesis guided by an mRNA-like portion of the tmRNA which ends with a stop codon and codes for a peptide sequence susceptible to proteolysis, thus allowing the bacteria to salvage stalled ribosomes and degrade ill-defined and potentially harmful protein products. In this article, we will recollect how structural studies have yielded a model for how the pre-translocation stages of trans-translation employing structural mimicry. We will also discuss possible models for

Place, publisher, year, edition, pages
2010. Vol. 7, no 5, 577-581 p.
Keyword [en]
trans-translation, tmRNA, SmpB, cryo electron microscopy, single particle, heterogeneity analysis
National Category
Industrial Biotechnology
Identifiers
URN: urn:nbn:se:kth:diva-31993ISI: 000288456500013Scopus ID: 2-s2.0-78649368975OAI: oai:DiVA.org:kth-31993DiVA: diva2:409442
Note

QC 20110408

Available from: 2011-04-08 Created: 2011-04-04 Last updated: 2017-06-09Bibliographically approved

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