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Mol Microbiol. 2011 Sep;81(6):1526-41. doi: 10.1111/j.1365-2958.2011.07793.x. Epub 2011 Aug 15.

RNase Y is responsible for uncoupling the expression of translation factor IF3 from that of the ribosomal proteins L35 and L20 in Bacillus subtilis.

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CNRS UPR 9073, Univ Paris Diderot, Sorbonne Paris Cité, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, 75005 Paris, France.


RNase Y is a novel endoribonuclease affecting global mRNA metabolism. We show that this nuclease affects the expression of the Bacillus subtilis infC-rpmI-rplT operon, encoding translation initiation factor IF3 and the ribosomal proteins L35 and L20. This operon is autoregulated by a complex L20-dependent transcription attenuation mechanism. L20 binds to a phylogenetically conserved domain on the 5' untranslated region of the infC mRNA which mimics the L20 binding sites on 23S rRNA. We have identified a second promoter (P1) upstream of the previously identified promoter (P2). The P1, but not the P2, readthrough transcript is stabilized in a strain depleted for RNase Y. However, under these conditions infC biosynthesis is repressed threefold. We show that the unprocessed P1 transcript is non-functional for IF3 translation but fully competent to express the co-transcribed ribosomal protein genes. RNase Y cleavage of the P1 transcript creates an entry site for the 5'-3' exonucleolytic activity of RNase J1 which degrades the infC mRNA when translation initiation efficiency is low. A second RNase Y cleavage is crucial for initiating degradation of the prematurely terminated infC leader RNAs, including the L20 operator complex, which permits efficient recycling of the L20 protein.

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