CsrA Represses Translation ofsdiA, Which Encodes theN-Acylhomoserine-<scp>l</scp>-Lactone Receptor of Escherichia coli, by Binding Exclusively within the Coding Region ofsdiAmRNA

Yakhnin, Helen; Baker, Carol S.; Berezin, Igor; Evangelista, Michael A.; Rassin, Alisa; Romeo, Tony; Babitzke, Paul

doi:10.1128/jb.05975-11

Cited by 49 publications

(66 citation statements)

References 47 publications

(85 reference statements)

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“…27 We suspect that in general, the strongest and presumably primary interaction of RsmA/CsrA proteins with target mRNAs takes place at or near the translation start site, while further appropriately spaced binding sites may have a modulating role. 4,26,27 As can be seen from the data of Table 1, mutations in the SD region not only affected post-transcriptional regulation by the Gac/Rsm system, but also influenced the translation efficiency in the wild-type over a 100-fold range. This variation mostly reflects differential translation initiation efficiencies but may also be due to differential mRNA stabilities.…”

Section: Discussionmentioning

confidence: 74%

“…For several E. coli mRNAs binding of CsrA to these GGA motifs has been demonstrated and, similarly, five GGA motifs in the 5' leader of hcnA mRNA of P. fluorescens have been shown to be involved in binding RsmA and RsmE. 4,[21][22][23][24][25][26][27] Highaffinity interactions have been analyzed by two approaches. First, a SELEX (systematic evolution of ligands by exponential enrichment) experiment generated a family of RNA molecules that were recognized by CsrA.…”

Section: Rna Pentaloop Structures As Effective Targets Of Regulators mentioning

confidence: 99%

“…When binding occurs at or near the ShineDalgarno (SD) sequence or within the coding sequence of a target mRNA, translation is repressed and this may be accompanied by enhanced mRNA degradation. [1][2][3][4] RsmA/CsrA proteins can also activate gene expression post-transcriptionally, either by binding to an upstream 5' region or, more commonly, by indirect mechanisms. 3,5 The 3D structures of the closely related Escherichia coli CsrA and Pseudomonas RsmA proteins have been determined.…”

Section: Introductionmentioning

confidence: 99%

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RNA pentaloop structures as effective targets of regulators belonging to the RsmA/CsrA protein family

et al. 2013

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Section: Discussionmentioning

confidence: 74%

Section: Rna Pentaloop Structures As Effective Targets Of Regulators mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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RNA pentaloop structures as effective targets of regulators belonging to the RsmA/CsrA protein family

et al. 2013

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“…To the best of our knowledge, this is the first report of such a phenomenon in pseudomonads. The presence of a similar unorthodox regulation mechanism has been reported in a study investigating the regulation of CsrA on the sdiA mRNA in E. coli (Yakhnin et al, 2011a). These authors demonstrated that CsrA could directly bind to two sites in the early coding sequence of that target gene, thus preventing translation by the ribosome.…”

Section: Discussionmentioning

confidence: 77%

Complex autoregulation of the post-transcriptional regulator RsmA in Pseudomonas aeruginosa

2015

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RsmA is a post-transcriptional RNA-binding protein that acts as a pleiotropic global regulator of mRNAs in the opportunistic pathogen Pseudomonas aeruginosa. Upon binding to its target, RsmA impedes the translation of the mRNA by the ribosome. The RsmA regulon affects over 500 genes, many of which have been identified as important in the pathogenicity of P. aeruginosa. Whilst the regulatory function of RsmA is relatively well characterized, the genetic regulation of rsmA itself at the transcriptional and translational levels remains poorly understood. Here, we show that RsmA is capable of self-regulation through an unorthodox mechanism. This regulation occurs via direct interaction of the protein with an RsmA-binding site located in the early portion of its coding sequence. To the best of our knowledge this is the first report of such an unusual regulation in pseudomonads.

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“…In Escherichia coli, CsrA activates glycolysis and central carbon pathways (7)(8)(9)(10)(11)(12)(13) and motility (14,15). Conversely, it represses gluconeogenesis (7), glycogen biosynthesis (16)(17)(18)(19)(20), biofilm formation (21)(22)(23)(24), the stringent response (25), and expression of genes involved in other stress resistance and stationary-phase processes, e.g., cstA, hfq, cel, sdiA, and nhaR (24,(26)(27)(28)(29)(30). Its effects on pathogenesis are complex.…”

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confidence: 99%

Circuitry Linking the Catabolite Repression and Csr Global Regulatory Systems of Escherichia coli

et al. 2016

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Cyclic AMP (cAMP) and the cAMP receptor protein (cAMP-CRP) and CsrA are the principal regulators of the catabolite repression and carbon storage global regulatory systems, respectively. cAMP-CRP controls the transcription of genes for carbohydrate metabolism and other processes in response to carbon nutritional status, while CsrA binds to diverse mRNAs and regulates translation, RNA stability, and/or transcription elongation. CsrA also binds to the regulatory small RNAs (sRNAs) CsrB and CsrC, which antagonize its activity. The BarA-UvrY two-component signal transduction system (TCS) directly activates csrB and csrC (csrB/C) transcription, while CsrA does so indirectly. We show that cAMP-CRP inhibits csrB/C transcription without negatively regulating phosphorylated UvrY (P-UvrY) or CsrA levels. A crp deletion caused an elevation in CsrB/C levels in the stationary phase of growth and increased the expression of csrB-lacZ and csrClacZ transcriptional fusions, although modest stimulation of CsrB/C turnover by the crp deletion partially masked the former effects. DNase I footprinting and other studies demonstrated that cAMP-CRP bound specifically to three sites located upstream from the csrC promoter, two of which overlapped the P-UvrY binding site. These two proteins competed for binding at the overlapping sites. In vitro transcription-translation experiments confirmed direct repression of csrC-lacZ expression by cAMP-CRP. In contrast, cAMP-CRP effects on csrB transcription may be mediated indirectly, as it bound nonspecifically to csrB DNA. In the reciprocal direction, CsrA bound to crp mRNA with high affinity and specificity and yet exhibited only modest, conditional effects on expression. Our findings are incorporated into an emerging model for the response of Csr circuitry to carbon nutritional status. IMPORTANCECsr (Rsm) noncoding small RNAs (sRNAs) CsrB and CsrC of Escherichia coli use molecular mimicry to sequester the RNA binding protein CsrA (RsmA) away from lower-affinity mRNA targets, thus eliciting major shifts in the bacterial lifestyle. CsrB/C transcription and turnover are activated by carbon metabolism products (e.g., formate and acetate) and by a preferred carbon source (glucose), respectively. We show that cAMP-CRP, a mediator of classical catabolite repression, inhibits csrC transcription by binding to the upstream region of this gene and also inhibits csrB transcription, apparently indirectly. We propose that glucose availability activates pathways for both synthesis and turnover of CsrB/C, thus shaping the dynamics of global signaling in response to the nutritional environment by poising CsrB/C sRNA levels for rapid response.T he Csr (carbon storage regulator) or Rsm (repressor of stationary-phase metabolites) system is a widely conserved bacterial posttranscriptional regulatory system (1-3). Its components, their functions, and the mechanisms by which the central regulator of this system, CsrA or RsmA, affects gene expression have been studied primarily in Gammaproteobacteria (4-6). The...

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CsrA Represses Translation ofsdiA, Which Encodes theN-Acylhomoserine-l-Lactone Receptor of Escherichia coli, by Binding Exclusively within the Coding Region ofsdiAmRNA

Cited by 49 publications

References 47 publications

RNA pentaloop structures as effective targets of regulators belonging to the RsmA/CsrA protein family

RNA pentaloop structures as effective targets of regulators belonging to the RsmA/CsrA protein family

Complex autoregulation of the post-transcriptional regulator RsmA in Pseudomonas aeruginosa

Circuitry Linking the Catabolite Repression and Csr Global Regulatory Systems of Escherichia coli

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