Comparison of the structure and regulation of the udp gene of Vibrio cholerae, Yersinia pseudotuberculosis, Salmonella typhimurium, and Escherichia coli

Zolotukhina, Maria; Ovcharova, I. V.; Eremina, Svetlana; Lopes, Liubov Errais; Mironov, A. S.

doi:10.1016/s0923-2508(03)00125-6

Cited by 27 publications

(27 citation statements)

References 30 publications

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“…Moreover, in a Δ cytR mutant, repression of udp–lux was eliminated (Fig. D), consistent with studies that showed repression of the udp gene by CytR in V. cholerae (Haugo and Watnick, ; Zolotukhina et al ., ).…”

Section: Resultsmentioning

confidence: 99%

Natural competence in Vibrio cholerae is controlled by a nucleoside scavenging response that requires CytR‐dependent anti‐activation

Antonova

Bernardy

Hammer

2012

Molecular Microbiology

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SummaryCompetence for genetic transformation in Vibrio cholerae is triggered by chitin-induced transcription factor TfoX and quorum sensing (QS) regulator HapR. Transformation requires expression of ComEA, described as a DNA receptor in other competent bacteria. A screen for mutants that poorly expressed a comEAluciferase fusion identified cytR, encoding the nucleoside scavenging cytidine repressor, previously shown in V. cholerae to be a biofilm repressor and positively regulated by TfoX, but not linked to transformation. A DcytR mutant was non-transformable and defective in expression of comEA and additional TfoXinduced genes, including pilA (transformation pseudopilus) and chiA-1 (chitinase). In Escherichia coli, 'anti-activation' of nucleoside metabolism genes, via protein-protein interactions between critical residues in CytR and CRP (cAMP receptor protein), is disrupted by exogenous cytidine. Amino acid substitutions of the corresponding V. cholerae CytR residues impaired expression of comEA, pilA and chiA-1, and halted DNA uptake; while exogenous cytidine hampered comEA expression levels and prevented transformation. Our results support a speculative model that when V. cholerae reaches high density on chitin, CytR-CRP interactions 'anti-activate' multiple genes, including a possible factor that negatively controls DNA uptake. Thus, a nucleoside scavenging mechanism couples nutrient stress and cell-cell signalling to natural transformation in V. cholerae as described in other bacterial pathogens.

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Section: Resultsmentioning

confidence: 99%

Natural competence in Vibrio cholerae is controlled by a nucleoside scavenging response that requires CytR‐dependent anti‐activation

Antonova

Bernardy

Hammer

2012

Molecular Microbiology

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“…Later the corresponding binding sites in the upstream regions of these genes, except nupC , were proposed. In other species, CytR was shown to regulate its own gene, cytR , in Salmonella typhimurium [14] and udp in Salmonella typhimurium , Yersinia pestis and Vibrio cholerae [15]. Since among the gamma-proteobacteria CytR is present only in E. coli and its close relatives (up to Vibrionales ), it has been suggested that cytR appeared in the Enterobacteriales due to horizontal transfer from the delta-Proteobacteria ( Geobacillus sp.)…”

Section: Introductionmentioning

confidence: 99%

Comparative Genomics of CytR, an Unusual Member of the LacI Family of Transcription Factors

Sernova

Gelfand

2012

PLoS ONE

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CytR is a transcription regulator from the LacI family, present in some gamma-proteobacteria including Escherichia coli and known not only for its cellular role, control of transport and utilization of nucleosides, but for a number of unusual structural properties. The present study addressed three related problems: structure of CytR-binding sites and motifs, their evolutionary conservation, and identification of new members of the CytR regulon. While the majority of CytR-binding sites are imperfect inverted repeats situated between binding sites for another transcription factor, CRP, other architectures were observed, in particular, direct repeats. While the similarity between sites for different genes in one genome is rather low, and hence the consensus motif is weak, there is high conservation of orthologous sites in different genomes (mainly in the Enterobacteriales) arguing for the presence of specific CytR-DNA contacts. On larger evolutionary distances candidate CytR sites may migrate but the approximate distance between flanking CRP sites tends to be conserved, which demonstrates that the overall structure of the CRP-CytR-DNA complex is gene-specific. The analysis yielded candidate CytR-binding sites for orthologs of known regulon members in less studied genomes of the Enterobacteriales and Vibrionales and identified a new candidate member of the CytR regulon, encoding a transporter named NupT (YcdZ).

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“…The udp gene encoding UPase constitutes a type of CytR regulon; the cAMP-CRP (cAMP receptor protein) complex, which acts as a co-repressor for the CytR protein, transcriptionally activates the udp gene. In E. coli, UPase is induced by cytidine but not by uridine (Thomsen et al, 1999;Esipov et al, 2002;Zolotukhina et al, 2003). In contrast, both uridine and cytidine induce UPase in S. typhimurium.…”

Section: Introductionmentioning

confidence: 91%

“…Their transcriptional regulations, protein structures and catalytic mechanisms have been extensively studied (Bzowska et al, 2000;Zolotukhina et al, 2003;Caradoc-Davies et al, 2004). NPases can be divided into three main types on the basis of substrate specificity: purine nucleoside phosphorylase (PNPase), uridine phosphorylase (UPase) and thymidine phosphorylase (TPase).…”

Section: Introductionmentioning

confidence: 99%

Induction of nucleoside phosphorylase in Enterobacter aerogenes and enzymatic synthesis of adenine arabinoside

Wei

Ding

Zhang

et al. 2008

J. Zhejiang Univ. Sci. B

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Nucleoside phosphorylases (NPases) were found to be induced in Enterobacter aerogenes DGO-04, and cytidine and cytidine 5′-monophosphate (CMP) were the best inducers. Five mmol/L to fifteen mmol/L cytidine or CMP could distinctly increase the activities of purine nucleoside phosphorylase (PNPase), uridine phosphorylase (UPase) and thymidine phosphorylase (TPase) when they were added into medium from 0 to 8 h. In the process of enzymatic synthesis of adenine arabinoside from adenine and uracil arabinoside with wet cells of Enterobacter aerogenes DGO-04 induced by cytidine or CMP, the reaction time could be shortened from 36 to 6 h. After enzymatic reaction the activity of NPase in the cells induced remained higher than that in the cells uninduced.

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Comparison of the structure and regulation of the udp gene of Vibrio cholerae, Yersinia pseudotuberculosis, Salmonella typhimurium, and Escherichia coli

Cited by 27 publications

References 30 publications

Natural competence in Vibrio cholerae is controlled by a nucleoside scavenging response that requires CytR‐dependent anti‐activation

Natural competence in Vibrio cholerae is controlled by a nucleoside scavenging response that requires CytR‐dependent anti‐activation

Comparative Genomics of CytR, an Unusual Member of the LacI Family of Transcription Factors

Induction of nucleoside phosphorylase in Enterobacter aerogenes and enzymatic synthesis of adenine arabinoside

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