Control of Expression of the Arginine Deiminase Operon of<i>Streptococcus gordonii</i>by CcpA and Flp

Dong, Yiqian; Chen, Yi-Ywan M.; Burne, Robert A.

doi:10.1128/jb.186.8.2511-2514.2004

Cited by 82 publications

(126 citation statements)

References 33 publications

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“…lactis CcpA ortholog PepR1 stimulates the expression of the prolidase-encoding pepQ gene and seems to affect the expression of pepX, pepI, and brnQ, which encode two other peptidases and a branched-chain amino acid transporter, respectively (779). A connection between CCR and amino acid metabolism also exists in Streptococcus gordonii and Streptococcus rattus, where the arginine deiminase operon is repressed by CcpA (195,298), and in B. subtilis, where CcpA stimulates the expression of the ilv-leu operon, which encodes the enzymes for the synthesis of branched-chain amino acids (810,882). A connection between CCR and the utilization of nitrogen sources was provided by the finding that the expression of rocG, which encodes the main glutamate dehydrogenase of B. subtilis, is subject to CcpA-mediated CCR (53).…”

Section: Catabolite Control Protein a Functions As A Catabolitementioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,187

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: Catabolite Control Protein a Functions As A Catabolitementioning

confidence: 99%

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

Deutscher

Francke

Postma

2006

Microbiol Mol Biol Rev

1,187

769

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“…CcpA has also been identified to function in the regulation of catabolic operons and catabolite repression in many Streptococcus spp. (1,17,59,77). CcpA has also shown to be required for biofilm formation in Streptococcus mutans (80).…”

mentioning

confidence: 99%

Catabolite Control Protein A (CcpA) Contributes to Virulence and Regulation of Sugar Metabolism in Streptococcus pneumoniae

2005

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We characterized the role of catabolite control protein A (ccpA) in the physiology and virulence of Streptococcus pneumoniae. S. pneumoniae has a large percentage of its genome devoted to sugar uptake and metabolism, and therefore, regulation of these processes is likely to be crucial for fitness in the nasopharynx and may play a role during invasive disease. In many bacteria, carbon catabolite repression (CCR) is central to such regulation, influencing hierarchical sugar utilization and growth rates. CcpA is the major transcriptional regulator in CCR in several gram-positive bacteria. We show that CcpA functions in CCR of lactose-inducible ␤-galactosidase activity in S. pneumoniae. CCR of maltose-inducible ␣-glucosidase, raffinose-inducible ␣-galactosidase, and cellobiose-inducible ␤-glucosidase is unaffected in the ccpA strain, suggesting that other regulators, possibly redundant with CcpA, control these systems. The ccpA strain is severely attenuated for nasopharyngeal colonization and lung infection in the mouse, establishing its role in fitness on these mucosal surfaces. Comparison of the cell wall fraction of the ccpA and wild-type strains shows that CcpA regulates many proteins in this compartment that are involved in central and intermediary metabolism, a subset of which are required for survival and multiplication in vivo. Both in vitro and in vivo defects were complemented by providing ccpA in trans. Our results demonstrate that CcpA, though not a global regulator of CCR in S. pneumoniae, is required for colonization of the nasopharynx and survival and multiplication in the lung.Carbon metabolism and its regulation are central to prokaryotic life. Sugars serve as the most facile source of carbon and energy, both of which are needed to replenish essential nucleotide cofactors and other metabolites in the cell. When faced with a wide variety of carbon and energy sources, a bacterium has to make metabolic decisions, opting for preferential use of one source over another in order to maintain optimal growth (70, 74).

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“…In oral biofilms, arginine is mainly metabolized by the arginine deiminase system (ADS) of oral bacteria, which yields citrulline, ornithine, CO 2 , ATP, and ammonia (Burne and Marquis, 2000). A substantial knowledge base about the physiology and genetics of the ADS in oral bacteria has been established (Marquis et al, 1987;Casiano-Colon and Marquis, 1988;Burne et al, 1991;Curran et al, 1998;Dong et al, 2004;Griswold et al, 2004;Zeng et al, 2006;Liu and Burne, 2009), but the role of arginine metabolism in oral ecology and oral health has not been thoroughly studied in humans. The main goal of this study was to explore the relationship between ADS activity and caries experience in children.…”

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confidence: 99%

Oral Arginine Metabolism May Decrease the Risk for Dental Caries in Children

Nascimento¹,

Liu²,

Kalra³

et al. 2013

J Dent Res

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Arginine metabolism by oral bacteria via the arginine deiminase system (ADS) increases the local pH, which can neutralize the effects of acidification from sugar metabolism and reduce the cariogenicity of oral biofilms. To explore the relationship between oral arginine metabolism and dental caries experience in children, we measured ADS activity in oral samples from 100 children and correlated it with their caries status and type of dentition. Supragingival dental plaque was collected from tooth surfaces that were caries-lesionfree (PF) and from dentinal (PD) and enamel (PE) caries lesions. Regardless of children's caries status or type of dentition, PF (378.6) had significantly higher ADS activity compared with PD (208.4; p < .001) and PE (194.8; p = .005). There was no significant difference in the salivary arginolytic activity among children with different caries status. Mixed-model analysis showed that plaque caries status is significantly associated with ADS activity despite children's age, caries status, and dentition (p < .001), with healthy plaque predicting higher ADS activity compared with diseased plaque. Plaque arginine metabolism varies greatly among children and tooth sites, which may affect their susceptibility to caries.

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Control of Expression of the Arginine Deiminase Operon ofStreptococcus gordoniiby CcpA and Flp

Abstract: In Streptococcus gordonii DL1, inactivation of the ccpA gene and a gene encoding an Fnr-like protein (Flp) demonstrated that CcpA was essential for carbohydrate catabolite repression and that Flp was required for optimal expression and anaerobic induction of the arginine deiminase system.

Cited by 82 publications

References 33 publications

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

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

Catabolite Control Protein A (CcpA) Contributes to Virulence and Regulation of Sugar Metabolism in Streptococcus pneumoniae

Oral Arginine Metabolism May Decrease the Risk for Dental Caries in Children

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