Abstract
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
Original language | English |
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Pages (from-to) | 577-581 |
Journal | RNA Biology |
Volume | 7 |
Issue number | 5 |
DOIs |
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Publication status | Published - 2010 |
Subject classification (UKÄ)
- Biological Sciences
Free keywords
- trans-translation
- tmRNA
- SmpB
- cryo electron microscopy
- single
- particle
- heterogeneity analysis