Both RNase E and RNase III control the stability of sodB mRNA upon translational inhibition by the small regulatory RNA RyhB

Previous work has demonstrated that iron-dependent variations in the steady-state concentration and translatability of sodB mRNA are modulated by the small regulatory RNA RyhB, the RNA chaperone Hfq and RNase E. In agreement with the proposed role of RNase E, we found that the decay of sodB mRNA is...

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Bibliographic Details
Published in:Nucleic acids research 2005-01, Vol.33 (5), p.1678-1689
Main Authors: Afonyushkin, Taras, Večerek, Branislav, Moll, Isabella, Bläsi, Udo, Kaberdin, Vladimir R.
Format: Article
Language:English
Subjects:
5' Untranslated Regions - chemistry
Bacterial Proteins - biosynthesis
Bacterial Proteins - genetics
Base Pairing
Base Sequence
Endoribonucleases - physiology
Escherichia coli - enzymology
Escherichia coli - genetics
Escherichia coli Proteins - metabolism
Gene Expression Regulation, Bacterial
Host Factor 1 Protein - metabolism
Models, Genetic
Molecular Sequence Data
Protein Biosynthesis
Ribonuclease III - physiology
Ribosomes - metabolism
RNA Processing, Post-Transcriptional
RNA Stability
RNA, Bacterial - metabolism
RNA, Messenger - metabolism
RNA, Untranslated - metabolism
Superoxide Dismutase - biosynthesis
Superoxide Dismutase - genetics
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Summary:Previous work has demonstrated that iron-dependent variations in the steady-state concentration and translatability of sodB mRNA are modulated by the small regulatory RNA RyhB, the RNA chaperone Hfq and RNase E. In agreement with the proposed role of RNase E, we found that the decay of sodB mRNA is retarded upon inactivation of RNase E in vivo, and that the enzyme cleaves within the sodB 5′-untranslated region (5′-UTR) in vitro, thereby removing the 5′ stem–loop structure that facilitates Hfq and ribosome binding. Moreover, RNase E cleavage can also occur at a cryptic site that becomes available upon sodB 5′-UTR/RyhB base pairing. We show that while playing an important role in facilitating the interaction of RyhB with sodB mRNA, Hfq is not tightly retained by the RyhB–sodB mRNA complex and can be released from it through interaction with other RNAs added in trans. Unlike turnover of sodB mRNA, RyhB decay in vivo is mainly dependent on RNase III, and its cleavage by RNase III in vitro is facilitated upon base pairing with the sodB 5′-UTR. These data are discussed in terms of a model, which accounts for the observed roles of RNase E and RNase III in sodB mRNA turnover.
ISSN:0305-1048
1362-4962
1362-4962
DOI:10.1093/nar/gki313