Regulation of the citrate synthase (gltA) gene of Escherichia coli in response to anaerobiosis and carbon supply: role of the arcA gene product

Park, Soon‐Jung; McCabe, J B; Turňa, Ján; Gunsalus, Robert P.

doi:10.1128/jb.176.16.5086-5092.1994

Cited by 89 publications

(93 citation statements)

References 31 publications

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“…Since the ArcA and/or the Fnr proteins are known to regulate several TCA cycle genes, including the sdhCDAB, mdh, gltA, acnA, and fumAC genes, in E. coli in response to anaerobiosis (6,8,(16)(17)(18)(19)27), we examined the effects of arcA and fnr gene deletions on sucA-lacZ and sdhCDAB-sucA-lacZ expression (Table 4). In neither the arcA strain nor the fnr strain did sucA-lacZ expression vary significantly compared to that of the wild-type strain grown under aerobic or anaerobic conditions.…”

Section: Resultsmentioning

confidence: 99%

“…A 1.375-kb XhoI-BamHI DNA fragment (Fig. 1) containing the sequence encoding the 235-amino-acid C-terminal region of SdhB, the 300-bp sdhB-sucA intergenic region, and the sequence encoding the 123-amino-acid N-terminal region of SucA was isolated from plasmid pJTSD1 (18) and cloned into pGEM11f(ϩ) (Promega Inc.) to give pSJP39. The EcoRI-BamHI fragment of pSJP39 containing the above DNA region was then transferred into pRS414 and pRS415 to generate the sucA-lacZ protein (pSJP42) and the sucA-lacZ operon (pSJP43) plasmids, respectively.…”

Section: Methodsmentioning

confidence: 99%

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Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter

1997

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The sucABCD genes of Escherichia coli encode subunits for two enzymes of the tricarboxylic acid (TCA) cycle, ␣-ketoglutarate dehydrogenase (sucAB) and succinyl coenzyme A synthetase (sucCD). To examine how these genes are expressed in response to changes in oxygen and carbon availability, a set of sucA-lacZ, sucC-lacZ, sdhCDAB-sucA-lacZ, and sdhC-lacZ fusions were constructed and analyzed in vivo. While the expression of a sucA-lacZ fusion was low under all cell growth conditions tested, the expression of the sucA gene from the upstream sdhC promoter was considerably higher and varied by up to 14-fold depending on the carbon substrate used. Expression of the sdhCDAB-sucA-lacZ fusion varied by fourfold in response to oxygen. In contrast, no expression was seen from a sucC-lacZ reporter fusion, indicating that no promoter immediately precedes the sucCD genes. Taken together, these findings demonstrate that the oxygen and carbon control of sucABCD gene expression occurs by transcriptional regulation of the upstream sdhC promoter. The weaker sucA promoter provides an additional low constitutive level of sucABCD gene expression to supplement transcription from the sdhC promoter. The negative control of sucABCD gene expression seen under anaerobic conditions, like that for the sdhCDAB genes, is provided by the arcA and fnr gene products. These findings establish that the differential expression of eight genes for three of the TCA cycle enzymes in E. coli is controlled from one regulatory element.The two tricarboxylic acid (TCA) cycle enzymes in Escherichia coli, ␣-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase (succinyl-CoA synthetase), are encoded by thesucAB and sucCD genes, respectively (4). ␣-Ketoglutarate dehydrogenase catalyzes the oxidative decarboxylation of ␣-ketoglutarate to generate succinyl-CoA and carbon dioxide, along with the production of NADH plus H ϩ (20). SuccinylCoA synthetase catalyzes the interconversion of succinyl-CoA and succinate, and this interconversion is accompanied by the production or hydrolysis of GTP (10, 15). Both TCA cycle enzymes participate in the cyclic flow of carbon from acetylCoA to carbon dioxide during aerobic cell growth conditions (4). This process provides reducing equivalents in the form of NADH for subsequent use in electron transport-linked phosphorylation reactions. Succinyl-CoA synthetase also participates in the noncyclic or branched pathway operative during anaerobic cell growth conditions to provide carbon intermediates for cell biosynthetic reactions (10, 15). The results of enzyme assays and two-dimensional protein gel electrophoresis studies indicate that the cellular synthesis of ␣-ketoglutarate dehydrogenase is suppressed by anaerobiosis and glucose and is induced by acetate or other oxidized carbon sources (1,5,24).The sucABCD genes are located at 16.7 min in the E. coli chromosome near the genes for two other TCA cycle enzymes, succinate dehydrogenase (sdhCDAB) and citrate synthase (gltA) (Fig. 1) (25). Little information is available concer...

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter

1997

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“…We propose that ArcA phosphate occupancy of ArcA sites 1 and/or 2 may provide for the repression of gltA gene expression during anaerobic conditions ( Fig. 1; Park et al, 1994). Recent studies by Park et al (1997) have also shown that expression of the genes for two other TCA cycle enzymes, ␣-ketoglutarate dehydrogenase (sucAB ) and succinylCoA synthetase (sucCD ), are also controlled from the sdhC promoter.…”

Section: Fnr Acts As a Negative Regulator Of Sdhc Promoter Expressionmentioning

confidence: 88%

Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB ) gene expression in Escherichia coli

Shen

Gunsalus

1997

Molecular Microbiology

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SummarySuccinate dehydrogenase (sdhCDAB ) gene expression in Escherichia coli is negatively regulated by the arcA and fnr gene products during anaerobic cell growth conditions. The controlled synthesis of this sole membrane-bound enzyme of the tricarboxylic acid cycle allows optimal participation in the aerobic electron transport pathway for the generation of energy via oxidative phosphorylation reactions. To understand how ArcA participates in the anaerobic repression of sdhCDAB expression, a family of sdhC-lacZ fusions was constructed and analysed in vivo. DNase I footprint and gel shift assays using purified ArcA protein revealed the location of four distinct and independent ArcA binding sites in the sdhC promoter region. ArcA sites, designated sites 1 and 2, are centred at ¹205 bp and ¹119 bp upstream of the sdhC promoter, respectively, whereas ArcA site 3 overlaps the ¹35 and ¹10 regions of the sdhC promoter. A fourth ArcA site is centred at þ 257 bp downstream of the sdhC promoter. They are bound with differing affinity by ArcA and ArcA phosphate. The in vivo studies, in combination with the in vitro studies, indicate that ArcA site 3 is necessary and sufficient for the ArcA-dependent repression of sdhC gene expression, while the DNA region containing ArcA site 2 contributes to maximal gene expression. The DNA-containing ArcA sites 1 and 4 provide minor roles in the ArcA regulation of sdhC expression. Lastly, the Fnr-dependent control of sdhCDAB gene expression was shown to occur independently of the ArcA and to require DNA sequences near the start of sdhC transcription.

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“…A more moderate inhibition occurs in the presence of excess glucose (160,170,193,212,(335)(336)(337)(338)(339)413).…”

Section: Limiting the Tricarboxylic Acid Cyclementioning

confidence: 99%

The Acetate Switch

Wolfe

2005

Microbiol Mol Biol Rev

1,069

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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Regulation of the citrate synthase (gltA) gene of Escherichia coli in response to anaerobiosis and carbon supply: role of the arcA gene product

Cited by 89 publications

References 31 publications

Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter

Aerobic regulation of the sucABCD genes of Escherichia coli, which encode alpha-ketoglutarate dehydrogenase and succinyl coenzyme A synthetase: roles of ArcA, Fnr, and the upstream sdhCDAB promoter

Role of multiple ArcA recognition sites in anaerobic regulation of succinate dehydrogenase (sdhCDAB ) gene expression in Escherichia coli

The Acetate Switch

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