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      RNA-binding proteins involved in post-transcriptional regulation in bacteria

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          Abstract

          Post-transcriptional regulation is a very important mechanism to control gene expression in changing environments. In the past decade, a lot of interest has been directed toward the role of small RNAs (sRNAs) in bacterial post-transcriptional regulation. However, sRNAs are not the only molecules controlling gene expression at this level, RNA-binding proteins (RBPs) play an important role as well. CsrA and Hfq are the two best studied bacterial proteins of this type, but recently, additional proteins involved in post-transcriptional control have been identified. This review focuses on the general working mechanisms of post-transcriptionally active RBPs, which include (i) adaptation of the susceptibility of mRNAs and sRNAs to RNases, (ii) modulating the accessibility of the ribosome binding site of mRNAs, (iii) recruiting and assisting in the interaction of mRNAs with other molecules and (iv) regulating transcription terminator/antiterminator formation, and gives an overview of both the well-studied and the newly identified proteins that are involved in post-transcriptional regulatory processes. Additionally, the post-transcriptional mechanisms by which the expression or the activity of these proteins is regulated, are described. For many of the newly identified proteins, however, mechanistic questions remain. Most likely, more post-transcriptionally active proteins will be identified in the future.

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          Most cited references146

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          Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli.

          RyhB is a small antisense regulatory RNA that is repressed by the Fur repressor and negatively regulates at least six mRNAs encoding Fe-binding or Fe-storage proteins in Escherichia coli. When Fe is limiting, RyhB levels rise, and target mRNAs are rapidly degraded. RyhB is very stable when measured after treatment of cells with the transcription inhibitor rifampicin, but is unstable when overall mRNA transcription continues. We propose that RyhB turnover is coupled to and dependent on pairing with the target mRNAs. Degradation of both mRNA targets and RyhB is dependent on RNase E and is slowed in degradosome mutants. RyhB requires the RNA chaperone Hfq. In the absence of Hfq, RyhB is unstable, even when general transcription is inhibited; degradation is dependent upon RNase E. Hfq and RNase E bind similar sites on the RNA; pairing may allow loss of Hfq and access by RNase E. Two other Hfq-dependent small RNAs, DsrA and OxyS, are also stable when overall transcription is off, and unstable when it is not, suggesting that they, too, are degraded when their target mRNAs are available for pairing. Thus, this large class of regulatory RNAs share an unexpected intrinsic mechanism for shutting off their action.
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            The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites.

            With a stepwise degradation and terminal labeling procedure the 3'-terminal sequence of E. coli 16S ribosomal RNA is shown to be Pyd-A-C-C-U-C-C-U-U-A(OH). It is suggested that this region of the RNA is able to interact with mRNA and that the 3'-terminal U-U-A(OH) is involved in the termination of protein synthesis through base-pairing with terminator codons. The sequence A-C-C-U-C-C could recognize a conserved sequence found in the ribosome binding sites of various coliphage mRNAs; it may thus be involved in the formation of the mRNA.30S subunit complex.
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              RNA chaperones and the RNA folding problem.

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                Author and article information

                Contributors
                Journal
                Front Microbiol
                Front Microbiol
                Front. Microbiol.
                Frontiers in Microbiology
                Frontiers Media S.A.
                1664-302X
                03 March 2015
                2015
                : 6
                : 141
                Affiliations
                [1]Centre of Microbial and Plant Genetics, Department of Molecular and Microbial Systems, KU Leuven Leuven, Belgium*
                Author notes

                Edited by: Martin G. Klotz, University of North Carolina at Charlotte, USA

                Reviewed by: Brian Stevenson, University of Kentucky, USA; Paul Babitzke, Penn State University, USA

                *Correspondence: Hans P. Steenackers, Centre of Microbial and Plant Genetics, Department of Molecular and Microbial Systems, KU Leuven, Kasteelpark Arenberg 20 bus 2460, 3000 Leuven, Belgium e-mail: hans.steenackers@ 123456biw.kuleuven.be

                This article was submitted to Microbial Physiology and Metabolism, a section of the journal Frontiers in Microbiology.

                Article
                10.3389/fmicb.2015.00141
                4347634
                25784899
                891ffc9c-961c-4ba0-9270-d9590ece287b
                Copyright © 2015 Van Assche, Van Puyvelde, Vanderleyden and Steenackers.

                This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

                History
                : 24 December 2014
                : 06 February 2015
                Page count
                Figures: 4, Tables: 1, Equations: 0, References: 156, Pages: 16, Words: 0
                Categories
                Microbiology
                Review Article

                Microbiology & Virology
                post-transcriptional regulation,rna-binding proteins,bacteria,working mechanisms,biotechnological applications,regulation of translation,stability regulation

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