Journal
RNA BIOLOGY
Volume 15, Issue 6, Pages 683-688Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15476286.2018.1454250
Keywords
A-site; ribosomes; co-translational mRNA decay; phylogeny; ribonuclease
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Funding
- Agence Nationale de la Recherche (ARNr-QC)
- Agence Nationale de la Recherche (CACSICE)
- Agence Nationale de la Recherche (DYNAMO)
- Centre National de la Recheche Scientifique [UMR8261]
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We recently identified a novel ribonuclease in Bacillus subtilis called Rae1 that cleaves mRNAs in a translation-dependent manner. Rae1 is a member of the NYN/PIN family of ribonucleases and is highly conserved in the Firmicutes, the Cyanobacteria and the chloroplasts of photosynthetic algae and plants. We have proposed a model in which Rae1 enters the A-site of ribosomes that are paused following translation of certain sequences that are still ill-defined. In the only case identified thus far, Rae1 cleaves between a conserved glutamate and lysine codon during translation of a short peptide called S1025. Certain other codons are also tolerated on either side of the cleavage site, but these are recognized less efficiently. The model of Rae1 docked in the A-site allows us to make predictions about which conserved residues may be important for recognition of mRNA, the tRNA in the adjacent P-site and binding to the 50S ribosome subunit.
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