Identification of Two
            <i>prpDBC</i>
            Gene Clusters in
            <i>Corynebacterium glutamicum</i>
            and Their Involvement in Propionate Degradation via the 2-Methylcitrate Cycle

Claes, Wilfried A.; Pühler, Alfred; Kalinowski, Jörn

doi:10.1128/jb.184.10.2728-2739.2002

Cited by 116 publications

(82 citation statements)

References 62 publications

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“…Thus, an alternative acetate assimilation pathway must exist, although AMP-ACS is an unlikely candidate: AMP-ACS activity has not been detected, and an obvious acs homolog does not appear in the genome sequence (152). Unlike E. coli, C. glutamicum requires the PTA-ACK pathway to grow on propionate (152) and no obvious prpE homolog appears in the genome (88). C. glutamicum appears to exert most of its control of the pta ack operon and the GB genes aceA and aceB primarily at the level of transcription initiation, which correlates with the presence of acetate in the environment (152,314,369,469,470).…”

Section: Pta-acka/amp-acs Acetate Switch Of the Gram-positivementioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,080

1,274

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To succeed, many cells must alternate between life-styles that permit rapid growth in the presence of abundant nutrients and ones that enhance survival in the absence of those nutrients. One such change in life-style, the “acetate switch,” occurs as cells deplete their environment of acetate-producing carbon sources and begin to rely on their ability to scavenge for acetate. This review explains why, when, and how cells excrete or dissimilate acetate. The central components of the “switch” (phosphotransacetylase [PTA], acetate kinase [ACK], and AMP-forming acetyl coenzyme A synthetase [AMP-ACS]) and the behavior of cells that lack these components are introduced. Acetyl phosphate (acetyl∼P), the high-energy intermediate of acetate dissimilation, is discussed, and conditions that influence its intracellular concentration are described. Evidence is provided that acetyl∼P influences cellular processes from organelle biogenesis to cell cycle regulation and from biofilm development to pathogenesis. The merits of each mechanism proposed to explain the interaction of acetyl∼P with two-component signal transduction pathways are addressed. A short list of enzymes that generate acetyl∼P by PTA-ACKA-independent mechanisms is introduced and discussed briefly. Attention is then directed to the mechanisms used by cells to “flip the switch,” the induction and activation of the acetate-scavenging AMP-ACS. First, evidence is presented that nucleoid proteins orchestrate a progression of distinct nucleoprotein complexes to ensure proper transcription of its gene. Next, the way in which cells regulate AMP-ACS activity through reversible acetylation is described. Finally, the “acetate switch” as it exists in selected eubacteria, archaea, and eukaryotes, including humans, is described

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Section: Pta-acka/amp-acs Acetate Switch Of the Gram-positivementioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,080

1,274

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“…0.66 kb) of pBV220C12Dncg12319 carrying the disrupted ncg12319 was then cloned into the vector pK18mobsacB 30) to generate the plasmid pK18mobsacB-ncg12319. This plasmid pK18mobsacB-ncg12319 was used to transform C. glutamicum RES167 8) by electroporation. Mutant screening was performed according to Schäfer et al 30) .…”

Section: Dna Manipulationmentioning

confidence: 99%

Genomic Analysis and Identification of Catabolic Pathways for Aromatic Compounds in Corynebacterium glutamicum

2005

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The catabolism of aromatic compounds in Corynebacterium glutamicum was investigated by genome data mining and by experimental analysis. Results indicated that C. glutamicum assimilated different aromatic compounds such as phenol, p-cresol, benzoate, 4-hydroxybenzoate, vanillate, vanillin, resorcinol, 3,5-dihydroxytoluene and 2,4-dihydroxybenzoate. Genome data indicated, and enzyme assays confirmed; the existence of multiple ring-cleavage pathways for the catabolism of central aromatic intermediates; the protocatechuate and catechol branches of the -ketoadipate pathway, two similar hydroxyquinol pathways and the gentisate pathway. Two putative hydroxyquinol 1,2-dioxygenase genes (ncg11113 and ncg12951) were cloned and functionally identified in Escherichia coli. The genes encoding enzymes for the conversion of phenol, benzoate, 3-hydroxybenzoate, 4-hydroxybenzoate and vanillate in the central -ketoadipate pathways were mapped on the chromosome of C. glutamicum. A unique 30-kb (approximately 1% of the entire genome) catabolic island that channels the degradation of various aromatic compounds was mapped to position 2525-2555 kb of the genome. The global analysis and characterization of aromatic degradation pathways provided new insights into the metabolic ability of C. glutamicum in addition to its well-known ability to produce various amino acids and vitamins.

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“…Besides, no HPr kinase/phosphatase system is found in the C. glutamicum genome. These differences in the molecular characteristics are likely reflected in the capacity of C. glutamicum to cometabolize glucose and a variety of carbon sources, including sugars, organic acids, and aromatic compounds without catabolite repression (17)(18)(19)(20)(21)(22)(23)(24), expect for a few cases (25)(26)(27).…”

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confidence: 99%

Involvement of Regulatory Interactions among Global Regulators GlxR, SugR, and RamA in Expression of ramA in Corynebacterium glutamicum

et al. 2013

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The central carbon metabolism genes in Corynebacterium glutamicum are under the control of a transcriptional regulatory network composed of several global regulators. It is known that the promoter region of ramA, encoding one of these regulators, interacts with its gene product, RamA, as well as with the two other regulators, GlxR and SugR, in vitro and/or in vivo. Although RamA has been confirmed to repress its own expression, the roles of GlxR and SugR in ramA expression have remained unclear. In this study, we examined the effects of GlxR binding site inactivation on expression of the ramA promoter-lacZ fusion in the genetic background of single and double deletion mutants of sugR and ramA. In the wild-type background, the ramA promoter activity was reduced to undetectable levels by the introduction of mutations into the GlxR binding site but increased by sugR deletion, indicating that GlxR and SugR function as the transcriptional activator and repressor, respectively. The marked repression of ramA promoter activity by the GlxR binding site mutations was largely compensated for by deletions of sugR and/or ramA. Furthermore, ramA promoter activity in the ramA-sugR double mutant was comparable to that in the ramA mutant but was significantly higher than that in the sugR mutant. Taken together, it is likely that the level of ramA expression is dynamically balanced by GlxR-dependent activation and repression by RamA along with SugR in response to perturbation of extracellular and/or intracellular conditions. These findings add multiple regulatory loops to the transcriptional regulatory network model in C. glutamicum.

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Identification of Two prpDBC Gene Clusters in Corynebacterium glutamicum and Their Involvement in Propionate Degradation via the 2-Methylcitrate Cycle

Cited by 116 publications

References 62 publications

The Acetate Switch

The Acetate Switch

Genomic Analysis and Identification of Catabolic Pathways for Aromatic Compounds in Corynebacterium glutamicum

Involvement of Regulatory Interactions among Global Regulators GlxR, SugR, and RamA in Expression of ramA in Corynebacterium glutamicum

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