CcpC-Dependent Regulation of<i>citB</i>and lmo0847 in<i>Listeria monocytogenes</i>

Kim, Hyun‐Jin; Mittal, Meghna; Sonenshein, Abraham L.

doi:10.1128/jb.188.1.179-190.2006

Cited by 23 publications

(42 citation statements)

References 63 publications

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“…A third trans-acting factor called CcpC is involved in CCR of the B. subtilis citB and citZ genes (which code for aconitase and citrate synthase, respectively) (386) and in CCR of the L. monocytogenes genes encoding a CitB ortholog and a presumed glutamine transporter (lmo0847) (402). However, CcpC is not a member of the LacI/GalR family but is a member of the LysR family of transcription regulators.…”

Section: What Are the Functions Of Ccpb And Ccpc?mentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,203

769

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SUMMARY The phosphoenolpyruvate(PEP):carbohydrate phosphotransferase system (PTS) is found only in bacteria, where it catalyzes the transport and phosphorylation of numerous monosaccharides, disaccharides, amino sugars, polyols, and other sugar derivatives. To carry out its catalytic function in sugar transport and phosphorylation, the PTS uses PEP as an energy source and phosphoryl donor. The phosphoryl group of PEP is usually transferred via four distinct proteins (domains) to the transported sugar bound to the respective membrane component(s) (EIIC and EIID) of the PTS. The organization of the PTS as a four-step phosphoryl transfer system, in which all P derivatives exhibit similar energy (phosphorylation occurs at histidyl or cysteyl residues), is surprising, as a single protein (or domain) coupling energy transfer and sugar phosphorylation would be sufficient for PTS function. A possible explanation for the complexity of the PTS was provided by the discovery that the PTS also carries out numerous regulatory functions. Depending on their phosphorylation state, the four proteins (domains) forming the PTS phosphorylation cascade (EI, HPr, EIIA, and EIIB) can phosphorylate or interact with numerous non-PTS proteins and thereby regulate their activity. In addition, in certain bacteria, one of the PTS components (HPr) is phosphorylated by ATP at a seryl residue, which increases the complexity of PTS-mediated regulation. In this review, we try to summarize the known protein phosphorylation-related regulatory functions of the PTS. As we shall see, the PTS regulation network not only controls carbohydrate uptake and metabolism but also interferes with the utilization of nitrogen and phosphorus and the virulence of certain pathogens.

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Section: What Are the Functions Of Ccpb And Ccpc?mentioning

confidence: 99%

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,203

769

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“…L. monocytogenes CcpC-His 6 was purified as previously described (24). For gel shift assays, a 237-bp DNA fragment corresponding to the lmo1568 promoter region was amplified by PCR using 32 P-labeled OMM050 and OMM064 as the forward and reverse primers and genomic DNA from L. monocytogenes EGD-e as the template.…”

Section: Methodsmentioning

confidence: 99%

“…To create a lacZ fusion to the region between lmo1569 and citZ, primer pair OMM015/OMM017 was used. The PCR products were digested with EcoRI and KpnI and ligated independently to pHK77 (24), which had been similarly digested. Plasmid pHK77 does not replicate in L. monocytogenes at elevated temperatures but integrates by homologous recombination at the nonessential intЈ-ЈcomK locus (24).…”

Section: Methodsmentioning

confidence: 99%

“…The PCR products were digested with EcoRI and KpnI and ligated independently to pHK77 (24), which had been similarly digested. Plasmid pHK77 does not replicate in L. monocytogenes at elevated temperatures but integrates by homologous recombination at the nonessential intЈ-ЈcomK locus (24). After transformation of E. coli and isolation of plasmid DNA, the insert was sequenced to confirm that it did not have PCR-generated mutations.…”

Section: Methodsmentioning

confidence: 99%

“…monocytogenes encodes a homolog of B. subtilis CcpC that binds tightly to the L. monocytogenes citB promoter region in vitro and represses citB transcription in vivo (24). Citrate inhibits the interaction of CcpC with the citB promoter region.…”

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confidence: 99%

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CcpC-Dependent Regulation of Citrate Synthase Gene Expression inListeria monocytogenes

2009

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Citrate synthase, the first and rate-limiting enzyme of the tricarboxylic acid branch of the Krebs cycle, was shown to be required for de novo synthesis of glutamate and glutamine in Listeria monocytogenes. The citrate synthase (citZ) gene was found to be part of a complex operon with the upstream genes lmo1569 and lmo1568. The downstream isocitrate dehydrogenase (citC) gene appears to be part of the same operon as well. Two promoters were shown to drive citZ expression, a distal promoter located upstream of lmo1569 and a proximal promoter located upstream of the lmo1568 gene. Transcription of citZ from both promoters was regulated by CcpC by interaction with a single site; assays of transcription in vivo and assays of CcpC binding in vitro revealed that CcpC interacts with and represses the proximal promoter that drives expression of the lmo1568, citZ, and citC genes and, by binding to the same site, prevents read-through transcription from the distal, lmo1569 promoter. Expression of the lmo1568 operon was not affected by the carbon source but was repressed during growth in complex medium by addition of glutamine.Listeria monocytogenes is a gram-positive food-borne bacterial parasite of mammals that causes listeriosis, an infection with a 30% mortality rate in susceptible humans that is characterized by fetoplacental and central nervous system infections and gastroenteritis (38). The risk group for listeriosis includes pregnant women, neonates, the elderly, and immunocompromised adults. Listeria infection has been an important model system for the study of host-pathogen interactions and mechanisms of intracellular parasitism (38). This bacterium is an intracellular pathogen that induces its own uptake by nonphagocytic cells and spreads from cell to cell via actinbased motility (4). Even though L. monocytogenes is able to grow intracellularly in a variety of mammalian cells, it is a facultative pathogen that can adapt to saprophytic growth on decaying soil vegetation (28). It is therefore interesting to examine how this bacterium senses the environment in order to regulate expression of its virulence determinants.Previous researchers have thoroughly investigated the molecular determinants of L. monocytogenes pathogenesis. The genes that encode all the currently known virulence factors are positively regulated by the transcriptional activator PrfA (3). These genes are repressed, however, when L. monocytogenes is grown in the presence of fermentable sugars (28). This carbon source-mediated repression of virulence genes does not involve CcpA, the global regulator of catabolite control in many gram-positive bacteria (2, 16, 36), but instead is due to effects of sugar metabolism on PrfA activity. Rapidly metabolized carbon sources alter the phosphorylation state of components of the phosphoenolpyruvate-dependent phosphotransferase system; one or more of these components appear to inhibit PrfA (17,27). Given that there is some uncertainty about the mechanisms that couple utilization of carbon sources and expression of...

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Metabolic determinants in Listeria monocytogenes anaerobic listeriolysin O production

et al. 2017

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Listeria monocytogenes is a human pathogen and a facultative anaerobe. To better understand how anaerobic growth affects L. monocytogenes pathogenesis, we first showed that anaerobic growth led to decreased growth and changes in surface morphology. Moreover, compared to aerobically grown bacteria, anaerobically grown L. monocytogenes established higher level of invasion but decreased intracellular growth and actin polymerization in cultured cells. The production of listeriolysin O (LLO) was significantly lower in anaerobic cultures—a phenotype observed in wild type and isogenic mutants lacking transcriptional regulators SigB or CodY or harboring a constitutively active PrfA. To explore potential regulatory mechanisms, we established that the addition of central carbon metabolism intermediates, such as acetate, citrate, fumarate, pyruvate, lactate, and succinate, led to an increase in LLO activity in the anaerobic culture supernatant. These results highlight the regulatory role of central carbon metabolism in L. monocytogenes pathogenesis under anaerobic conditions.

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CcpC-Dependent Regulation ofcitBand lmo0847 inListeria monocytogenes

Cited by 23 publications

References 63 publications

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

How Phosphotransferase System-Related Protein Phosphorylation Regulates Carbohydrate Metabolism in Bacteria

CcpC-Dependent Regulation of Citrate Synthase Gene Expression inListeria monocytogenes

Metabolic determinants in Listeria monocytogenes anaerobic listeriolysin O production

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