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- Publisher
- Wiley
- Copyright
- Copyright © 2013 Wiley Periodicals, Inc
- ISSN
- 0261-4189
- eISSN
- 1460-2075
- DOI
- 10.1093/emboj/17.16.4790
- pmid
- 9707438
- Publisher site
- See Article on Publisher Site
Abstract
The hypothesis generally proposed to explain the stabilizing effect of translation on many bacterial mRNAs is that ribosomes mask endoribonuclease sites which control the mRNA decay rate. We present the first demonstration that ribosomes interfere with a particular RNase E processing event responsible for mRNA decay. These experiments used an rpsO mRNA deleted of the translational operator where ribosomal protein S15 autoregulates its synthesis. We demonstrate that ribosomes inhibit the RNase E cleavage, 10 nucleotides downstream of the rpsO coding sequence, responsible for triggering the exonucleolytic decay of the message mediated by polynucleotide phosphorylase. Early termination codons and insertions which increase the length of ribosome‐free mRNA between the UAA termination codon and this RNase E site destabilize the translated mRNA and facilitate RNase E cleavage, suggesting that ribosomes sterically inhibit RNase E access to the processing site. Accordingly, a mutation which reduces the distance between these two sites stabilizes the mRNA. Moreover, an experiment showing that a 10 nucleotide insertion which destabilizes the untranslated mRNA does not affect mRNA stability when it is inserted in the coding sequence of a translated mRNA demonstrates that ribosomes can mask an RNA feature, 10–20 nucleotides upstream of the processing site, which contributes to the RNase E cleavage efficiency.
Journal
The EMBO Journal – Wiley
Published: May 17, 1999
Keywords: ; ; ;