Condon, CiaranPiton, JeremieBraun, Frederique2018-12-132018-12-132018-12-132018-01-0110.1080/15476286.2018.1454250https://infoscience.epfl.ch/handle/20.500.14299/152491WOS:000444092300002We 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.Biochemistry & Molecular BiologyBiochemistry & Molecular Biologya-siteribosomesco-translational mrna decayphylogenyribonucleasemessenger-rna cleavagebacillus-subtilistranslation elongationendoribonucleasebacteriatext::journal::journal article::research article