CcpA-Dependent Carbon Catabolite Repression in Bacteria

Warner, Jessica B.; Lolkema, Juke S.

doi:10.1128/mmbr.67.4.475-490.2003

Cited by 233 publications

(227 citation statements)

References 44 publications

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“…Analysis of the mannose PTS revealed that the genes encoding the EIIABCD Man were consistently highly expressed, regardless of the carbohydrate source (Fig. 1), which is consistent with the important regulatory roles in Gram-positive bacteria established for EII Man (24,25). Similarly, EIIABC Fru seemed consistently highly expressed (Fig.…”

Section: Discussionsupporting

confidence: 58%

Global analysis of carbohydrate utilization by Lactobacillus acidophilus using cDNA microarrays

Barrangou

Azcarate‐Peril

Duong

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

181

168

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The transport and catabolic machinery involved in carbohydrate utilization by Lactobacillus acidophilus was characterized genetically by using whole-genome cDNA microarrays. Global transcriptional profiles were determined for growth on glucose, fructose, sucrose, lactose, galactose, trehalose, raffinose, and fructooligosaccharides. Hybridizations were carried out by using a roundrobin design, and microarray data were analyzed with a two-stage mixed model ANOVA. Differentially expressed genes were visualized by hierarchical clustering, volcano plots, and contour plots. Overall, only 63 genes (3% of the genome) showed a >4-fold induction. Specifically, transporters of the phosphoenolpyruvate: sugar transferase system were identified for uptake of glucose, fructose, sucrose, and trehalose, whereas ATP-binding cassette transporters were identified for uptake of raffinose and fructooligosaccharides. A member of the LacS subfamily of galactosidepentose hexuronide translocators was identified for uptake of galactose and lactose. Saccharolytic enzymes likely involved in the metabolism of monosaccharides, disaccharides, and polysaccharides into substrates of glycolysis were also found, including enzymatic machinery of the Leloir pathway. The transcriptome appeared to be regulated by carbon catabolite repression. Although substrate-specific carbohydrate transporters and hydrolases were regulated at the transcriptional level, genes encoding regulatory proteins CcpA, Hpr, HprK͞P, and EI were consistently highly expressed. Genes central to glycolysis were among the most highly expressed in the genome. Collectively, microarray data revealed that coordinated and regulated transcription of genes involved in sugar uptake and metabolism is based on the specific carbohydrate provided. L. acidophilus's adaptability to environmental conditions likely contributes to its competitive ability for limited carbohydrate sources available in the human gastrointestinal tract.ATP-binding cassette ͉ carbon catabolite repression ͉ fructooligosaccharide ͉ galactoside-pentose hexuronide

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Section: Discussionsupporting

confidence: 58%

Global analysis of carbohydrate utilization by Lactobacillus acidophilus using cDNA microarrays

Barrangou

Azcarate‐Peril

Duong

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

181

168

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“…The CCR in L. plantarum NCC245 probably acts through the principal transcriptional regulator CcpA (Warner & Lolkema, 2003), which binds to its operator site, cre. A typical cre element (Miwa et al, 2000) was identified in the rha promoter region (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…2). This cis-acting element (Miwa et al, 2000) is a binding site of the major CCR regulator CcpA (Warner & Lolkema, 2003).…”

Section: Selection Of Bacteria With A-l-rhamnosidase Activitymentioning

confidence: 99%

Physiological and biochemical characterization of the two α-l-rhamnosidases of Lactobacillus plantarum NCC245

et al. 2009

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This work is believed to be the first report on the physiological and biochemical characterization of a-L-rhamnosidases in lactic acid bacteria. A total of 216 strains representing 37 species and eight genera of food-grade bacteria were screened for a-L-rhamnosidase activity. The majority of positive bacteria (25 out of 35) were Lactobacillus plantarum strains, and activity of the L. plantarum strain NCC245 was examined in more detail. The analysis of a-L-rhamnosidase activity under different growth conditions revealed dual regulation of the enzyme activity, involving carbon catabolite repression and induction: the enzyme activity was downregulated by glucose and upregulated by L-rhamnose. The expression of the two a-L-rhamnosidase genes rhaB1 and rhaB2 and two predicted permease genes rhaP1 and rhaP2, identified in a probable operon rhaP2B2P1B1, was repressed by glucose and induced by L-rhamnose, showing regulation at the transcriptional level. The two a-L-rhamnosidase genes were overexpressed and purified from Escherichia coli. RhaB1 activity was maximal at 50 6C and at neutral pH and RhaB2 maximal activity was detected at 60 6C and at pH 5, with high residual activity at 70 6C. Both enzymes showed a preference for the a-1,6 linkage of L-rhamnose to b-D-glucose, hesperidin and rutin being their best substrates, but, surprisingly, no activity was detected towards the a-1,2 linkage in naringin under the tested conditions. In conclusion, we identified and characterized the strain L. plantarum NCC245 and its two a-L-rhamnosidase enzymes, which might be applied for improvement of bioavailability of health-beneficial polyphenols, such as hesperidin, in humans.

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“…Within EII, EIIA accepts the phosphoryl group from HPr and donates it to EIIB, whereupon EIIC mediates sugar translocation. In addition to controlling sugar translocation, the phosphorylation state of PTS proteins is associated with regulation of metabolic pathways and signaling in bacterial cells (4)(5)(6)(7)(8).…”

mentioning

confidence: 99%

Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein

Teplyakov

Lim

Zhu

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

179

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sugar transport ͉ phosphorylation ͉ x-ray crystallography T he phosphoenolpyruvate (PEP):sugar phosphotransferase system (PTS) (1) catalyzes the synchronized uptake and phosphorylation of a number of carbohydrates in eubacteria (group translocation) (2, 3). With some variations, the PTS comprises three proteins. In the cytoplasm, PEP phosphorylates enzyme I (EI), which then transfers the phosphoryl group to the histidine phosphocarrier protein, HPr. From HPr, the phosphoryl group is transferred to various sugar-specific membrane associated transporters [enzyme II (EII)], each comprising two cytoplasmic domains, EIIA and EIIB, and an integral membrane domain EIIC. Within EII, EIIA accepts the phosphoryl group from HPr and donates it to EIIB, whereupon EIIC mediates sugar translocation. In addition to controlling sugar translocation, the phosphorylation state of PTS proteins is associated with regulation of metabolic pathways and signaling in bacterial cells (4-8).The Ϸ64-kDa EI is a homodimer, which is more tightly associated at the phosphorylated state than the unphosphorylated state (9-14). The phosphorylation by PEP requires Mg 2ϩ and targets the N atom of His-189 (numbering scheme of EI from Escherichia coli) (15). The dimer association rate constant is two to three orders of magnitude slower than typical rates measured for other dimeric proteins, suggesting that oligomerization is accompanied by major conformational rearrangements (13,16,17). The monomer-dimer equilibrium has been studied in vitro by various methods (18-21), and it has been proposed that the transition plays a regulatory role in the PEP:sugar phosphotransferase system. Yet, transient kinetic studies indicated that the EI dimer phosphorylates HPr without dissociating into monomers (17).Proteolytic cleavage of EI produces two domains (22, 23). The EI N-terminal domain (EIN, residues 1-230) contains the residue that transfers the phosphoryl group, 24) and the HPr-binding domain, whereas the EI C-terminal domain (EIC, residues 261-575) binds PEP in the presence of Mg 2ϩ (the PEP-binding domain) (22,25) and mediates dimerization (26,27). Site-directed mutagenesis showed that Cys-502, located on EIC, is essential for phosphorylation of His-189 by PEP (28). The structure of EIN from E. coli has been determined by x-ray crystallography (29) and NMR spectroscopy (30).

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CcpA-Dependent Carbon Catabolite Repression in Bacteria

Cited by 233 publications

References 44 publications

Global analysis of carbohydrate utilization by Lactobacillus acidophilus using cDNA microarrays

Global analysis of carbohydrate utilization by Lactobacillus acidophilus using cDNA microarrays

Physiological and biochemical characterization of the two α-l-rhamnosidases of Lactobacillus plantarum NCC245

Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein

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