The CAP Modulon

Busby, Stephen; Kolb, Annie

doi:10.1007/978-1-4684-8601-8_12

Cited by 60 publications

(33 citation statements)

References 143 publications

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“…To our knowledge, a CRP role in activation by direct binding this far upstream of the promoter has not been previously reported. The binding sites for CRP found for any previously characterized promoters, including galP1, lacP1, malTp, ansB, and uhpTp, are centered not farther than Ϫ121.5 bp upstream of their transcription start sites (27)(28)(29)(30). For activation of papBA in E. coli, where CRP binding at Ϫ215.5 bp is the most exceptional distant binding reported, CRP without Lrp (leucineresponsive regulatory protein) provides little activation.…”

Section: Discussionmentioning

confidence: 94%

SmcR and Cyclic AMP Receptor Protein Coactivate Vibrio vulnificus vvpE Encoding Elastase through the RpoS-dependent Promoter in a Synergistic Manner

Jeong

Lee

et al. 2003

Journal of Biological Chemistry

146

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The putative virulence factors of Vibrio vulnificus include an elastase, the gene product of vvpE. We previously demonstrated that vvpE expression is differentially directed by two different promoters in a growth phase-dependent manner. The activity of the stationaryphase promoter (promoter S (PS)) is dependent on RpoS and is also under the positive control of cyclic AMP receptor protein (CRP). In this study, primer extension analyses revealed that SmcR, the Vibrio harveyi LuxR homolog, is also involved in the regulation of vvpE transcription by activating PS. Although the influence of CRP on PS is mediated by SmcR, the level of PS activity observed when CRP and SmcR function together was found to be greater than the sum of the PS activities achieved by each activator alone. Western blot analyses demonstrated that the cellular levels of RpoS, CRP, and SmcR were not significantly affected by one other, indicating that CRP and SmcR function cooperatively to activate PS rather than sequentially in a regulatory cascade. The binding sites for CRP and SmcR were mapped based on a deletion analysis of the vvpE promoter region and confirmed by in vitro DNase I protection assays. The binding sites for CRP and SmcR were juxtapositioned and centered 220 and 198 bp upstream of the transcription start site of PS, respectively. Accordingly, these results reveal that CRP and SmcR function synergistically to coactivate the expression of vvpE by the RpoSdependent promoter (PS) and that the activators exert their effect by directly binding to the promoter in the stationary phase.The pathogenic marine bacterium Vibrio vulnificus is the causative agent of food-borne diseases, including life-threatening septicemia and possibly gastroenteritis, in individuals with underlying predisposed conditions such as liver damage, excess levels of iron, and immunocompromised conditions. Wound infections also result from exposure to seawater or from the handling of shellfish contaminated with V. vulnificus. The mortality from septicemia is very high (Ͼ50%), and death can occur within 1-2 days after the first signs of illness. Several potential virulence factors, including an endotoxin, polysaccharide capsule, iron-sequestering systems, cytolytic hemolysin, elastase, phospholipase A 2 , and other exotoxins, have been identified in V. vulnificus (for recent reviews, see Refs. 1 and 2).The elastase activity is from a neutral metalloprotease and represents the major proteolytic activity of V. vulnificus (3, 4). Our previous study revealed the existence of at least two proteases that are produced by V. vulnificus (5). Therefore, vvpE was designed to differentiate the elastase gene from other genes encoding other potential proteases of V. vulnificus (5). As such, a gene encoding the V. vulnificus elastase was recently cloned and sequenced by us (5) and by others (6). The deduced gene product was predicted to be a 609-amino acid polypeptide, and the mature elastase is a 45-kDa protein consisting of 413 amino acids generated by the deletion of the N-termi...

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Section: Discussionmentioning

confidence: 94%

SmcR and Cyclic AMP Receptor Protein Coactivate Vibrio vulnificus vvpE Encoding Elastase through the RpoS-dependent Promoter in a Synergistic Manner

Jeong

Lee

et al. 2003

Journal of Biological Chemistry

146

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“…CRP binds to a palindromic sequence (TGTGAN 6 TCACA) in the promoters of target genes and, depending on the distance between the binding site and the transcriptional start site, enhances or restricts recruitment of ribonucleic acid (RNA) polymerase [reviewed in (10,11)]. In addition to binding to target promoters, ChIP-chip analysis of E. coli CRP uncovered an extensive background pattern of low affinity sites suggesting that CRP may have an additional role as a more general chromosomal organizer (12).…”

Section: Introductionmentioning

confidence: 99%

Genomic mapping of cAMP receptor protein (CRP^Mt) inMycobacterium tuberculosis: relation to transcriptional start sites and the role of CRP^Mtas a transcription factor

Kahramanoglou¹,

Cortes²,

Matange³

et al. 2014

Nucleic Acids Res

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Chromatin immunoprecipitation identified 191 binding sites of Mycobacterium tuberculosis cAMP receptor protein (CRPMt) at endogenous expression levels using a specific α-CRPMt antibody. Under these native conditions an equal distribution between intragenic and intergenic locations was observed. CRPMt binding overlapped a palindromic consensus sequence. Analysis by RNA sequencing revealed widespread changes in transcriptional profile in a mutant strain lacking CRPMt during exponential growth, and in response to nutrient starvation. Differential expression of genes with a CRPMt-binding site represented only a minor portion of this transcriptional reprogramming with ∼19% of those representing transcriptional regulators potentially controlled by CRPMt. The subset of genes that are differentially expressed in the deletion mutant under both culture conditions conformed to a pattern resembling canonical CRP regulation in Escherichia coli, with binding close to the transcriptional start site associated with repression and upstream binding with activation. CRPMt can function as a classical transcription factor in M. tuberculosis, though this occurs at only a subset of CRPMt-binding sites.

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“…E. coli CRP is activated by binding cAMP and controls aspects of carbon metabolism and virulence gene expression and may act as a more general chromosome organizer (9–11). In E.…”

Section: Introductionmentioning

confidence: 99%

Mycobacterium tuberculosis cAMP Receptor Protein (Rv3676) Differs from the Escherichia coli Paradigm in Its cAMP Binding and DNA Binding Properties and Transcription Activation Properties

Stapleton

Haq

Hunt

et al. 2010

Journal of Biological Chemistry

120

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The pathogen Mycobacterium tuberculosis produces a burst of cAMP upon infection of macrophages. Bacterial cyclic AMP receptor proteins (CRP) are transcription factors that respond to cAMP by binding at target promoters when cAMP concentrations increase. Rv3676 (CRPMt) is a CRP family protein that regulates expression of genes (rpfA and whiB1) that are potentially involved in M. tuberculosis persistence and/or emergence from the dormant state. Here, the CRPMt homodimer is shown to bind two molecules of cAMP (one per protomer) at noninteracting sites. Furthermore, cAMP binding by CRPMt was relatively weak, entropy driven, and resulted in a relatively small enhancement in DNA binding. Tandem CRPMt-binding sites (CRP1 at −58.5 and CRP2 at −37.5) were identified at the whiB1 promoter (PwhiB1). In vitro transcription reactions showed that CRP1 is an activating site and that CRP2, which was only occupied in the presence of cAMP or at high CRPMt concentrations in the absence of cAMP, is a repressing site. Binding of CRPMt to CRP1 was not essential for open complex formation but was required for transcription activation. Thus, these data suggest that binding of CRPMt to the PwhiB1 CRP1 site activates transcription at a step after open complex formation. In contrast, high cAMP concentrations allowed occupation of both CRP1 and CRP2 sites, resulting in inhibition of open complex formation. Thus, M. tuberculosis CRP has evolved several distinct characteristics, compared with the Escherichia coli CRP paradigm, to allow it to regulate gene expression against a background of high concentrations of cAMP.

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The CAP Modulon

Cited by 60 publications

References 143 publications

SmcR and Cyclic AMP Receptor Protein Coactivate Vibrio vulnificus vvpE Encoding Elastase through the RpoS-dependent Promoter in a Synergistic Manner

SmcR and Cyclic AMP Receptor Protein Coactivate Vibrio vulnificus vvpE Encoding Elastase through the RpoS-dependent Promoter in a Synergistic Manner

Genomic mapping of cAMP receptor protein (CRP^Mt) inMycobacterium tuberculosis: relation to transcriptional start sites and the role of CRP^Mtas a transcription factor

Mycobacterium tuberculosis cAMP Receptor Protein (Rv3676) Differs from the Escherichia coli Paradigm in Its cAMP Binding and DNA Binding Properties and Transcription Activation Properties

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The CAP Modulon

Cited by 60 publications

References 143 publications

SmcR and Cyclic AMP Receptor Protein Coactivate Vibrio vulnificus vvpE Encoding Elastase through the RpoS-dependent Promoter in a Synergistic Manner

SmcR and Cyclic AMP Receptor Protein Coactivate Vibrio vulnificus vvpE Encoding Elastase through the RpoS-dependent Promoter in a Synergistic Manner

Genomic mapping of cAMP receptor protein (CRPMt) inMycobacterium tuberculosis: relation to transcriptional start sites and the role of CRPMtas a transcription factor

Mycobacterium tuberculosis cAMP Receptor Protein (Rv3676) Differs from the Escherichia coli Paradigm in Its cAMP Binding and DNA Binding Properties and Transcription Activation Properties

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Genomic mapping of cAMP receptor protein (CRP^Mt) inMycobacterium tuberculosis: relation to transcriptional start sites and the role of CRP^Mtas a transcription factor