Regulation of fumarase (fumB) gene expression in Escherichia coli in response to oxygen, iron and heme availability: role of the arcA, fur, and hemA gene products

Tseng, Chih-Yung

doi:10.1016/s0378-1097(97)00455-2

Cited by 23 publications

(30 citation statements)

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“…1). These physiological functions coincide with the results of studies using various fum-lacZ reporter fusions in which the level of fumA gene expression was seven-to eightfold higher than that of fumB even under anaerobic condition (20,29). As the three fumarase activities in E. coli are regulated by oxygen differently, the cell utilizes a complex strategy for adaptation to diverse environmental oxygen levels.…”

Section: Discussionsupporting

confidence: 84%

“…Their differing affinities for fumarate and malate suggest that they function in reciprocal roles either in the overall oxidation of fumarate via the citric acid cycle (by FumA) or in the ultimate reduction of malate by providing fumarate as an anaerobic electron acceptor (by FumB) (32,34). Also, it was previously shown that the fumA and fumC genes were expressed at higher levels under aerobic than anaerobic conditions, whereas fumB was expressed under anaer- obic condition (20,29,32). In this study, we performed a more detailed analysis of three fumarase activities under different oxygen levels.…”

Section: Discussionmentioning

confidence: 99%

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Oxygen- and Growth Rate-Dependent Regulation of Escherichia coli Fumarase (FumA, FumB, and FumC) Activity

Tseng

Lin

et al. 2001

J Bacteriol

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Escherichia coli contains three biochemically distinct fumarases which catalyze the interconversion of fumarate to L-malate in the tricarboxylic acid cycle. Batch culture studies indicated that fumarase activities varied according to carbon substrate and cell doubling time. Growth rate control of fumarase activities in the wild type and mutants was demonstrated in continuous culture; FumA and FumC activities were induced fourto fivefold when the cell growth rate (k) was lowered from 1.2/h to 0.24/h at 1 and 21% O 2 , respectively. There was a twofold induction of FumA and FumC activities when acetate was utilized instead of glucose as the sole carbon source. However, these fumarase activities were still shown to be under growth rate control. Thus, the activity of the fumarases is regulated by the cell growth rate and carbon source utilization independently. Further examination of FumA and FumC activities in a cya mutant suggested that growth rate control of FumA and FumC activities is cyclic AMP dependent. Although the total fumarase activity increased under aerobic conditions, the individual fumarase activities varied under different oxygen levels. While FumB activity was maximal during anaerobic growth (k ‫؍‬ 0.6/h), FumA was the major enzyme under anaerobic cell growth, and the maximum activity was achieved when oxygen was elevated to 1 to 2%. Further increase in the oxygen level caused inactivation of FumA and FumB activities by the high oxidized state, but FumC activity increased simultaneously when the oxygen level was higher than 4%. The same regulation of the activities of fumarases in response to different oxygen levels was also found in mutants. Therefore, synthesis of the three fumarase enzymes is controlled in a hierarchical fashion depending on the environmental oxygen that the cell encounters.

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Section: Discussionsupporting

confidence: 84%

Section: Discussionmentioning

confidence: 99%

Oxygen- and Growth Rate-Dependent Regulation of Escherichia coli Fumarase (FumA, FumB, and FumC) Activity

Tseng

Lin

et al. 2001

J Bacteriol

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“…The results of this analysis indicate that seven sequenced S. enterica isolates from five serovars (Typhi, Paratyphi A and C, Choleraesuis, and Gallinarum) have lost the ability to reduce at least one of the following oxidized substrates in order to maintain a respiratory metabolism under anaerobic conditions: tetrathionate (Typhi, Paratyphi A, and Gallinarum), thiosulfate (Typhi and Paratyphi A), sulfite (Gallinarum), dimethyl sulfoxide (DMSO; Paratyphi A), and trimethylamine N-oxide (TMAO; Typhi, Choleraesuis, Gallinarum, and Paratyphi C). In addition, the gene cluster encoding malate dehydratase FumB, which can provide fumarate as an electron acceptor under anaerobic conditions (75), is incomplete in serovars Typhi, Paratyphi A, Javiana, Schwarzengrund, and Saintpaul SARA29. Similarly, the nitrate-inducible formate dehydrogenase, which serves as a major electron donor during anaerobic respiration (5), is predicted to be inactive in serovars Choleraesuis, Typhi, and Paratyphi A, B, and C. As the enzymes for tetrathionate, thiosulfate, and DMSO reduction use a molybdenum cofactor, the cbi operon of coenzyme B12 biosynthesis was examined and found to be incomplete in serovars Typhi and Paratyphi A, Choleraesuis, and Gallinarum.…”

Section: ) (33)mentioning

confidence: 99%

Comparative Genomics of 28 Salmonella enterica Isolates: Evidence for CRISPR-Mediated Adaptive Sublineage Evolution

et al. 2011

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Despite extensive surveillance, food-borne Salmonella enterica infections continue to be a significant burden on public health systems worldwide. As the S. enterica species comprises sublineages that differ greatly in antigenic representation, virulence, and antimicrobial resistance phenotypes, a better understanding of the species' evolution is critical for the prediction and prevention of future outbreaks. The roles that virulence and resistance phenotype acquisition, exchange, and loss play in the evolution of S. enterica sublineages, which to a certain extent are represented by serotypes, remains mostly uncharacterized. Here, we compare 17 newly sequenced and phenotypically characterized nontyphoidal S. enterica strains to 11 previously sequenced S. enterica genomes to carry out the most comprehensive comparative analysis of this species so far. These phenotypic and genotypic data comparisons in the phylogenetic species context suggest that the evolution of known S. enterica sublineages is mediated mostly by two mechanisms, (i) the loss of coding sequences with known metabolic functions, which leads to functional reduction, and (ii) the acquisition of horizontally transferred phage and plasmid DNA, which provides virulence and resistance functions and leads to increasing specialization. Matches between S. enterica clustered regularly interspaced short palindromic repeats (CRISPR), part of a defense mechanism against invading plasmid and phage DNA, and plasmid and prophage regions suggest that CRISPR-mediated immunity could control short-term phenotype changes and mediate long-term sublineage evolution. CRISPR analysis could therefore be critical in assessing the evolutionary potential of S. enterica sublineages and aid in the prediction and prevention of future S. enterica outbreaks.

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“…Of these 30 genes, only fumarate hydratase (Cj1364) and Cj0859c (hypothetical) were previously shown to have reduced expression in the wild-type strain under iron limitation and thus might be directly or indirectly regulated by Fur. Fumarase activity has also been shown to be iron responsive in Pseudomonas aeruginosa, Pasteurella multocida and E. coli (Hassett et al, 1997;Paustian et al, 2001;Tseng, 1997).…”

Section: Iron Limitedmentioning

confidence: 99%

Campylobacter jejuni gene expression in response to iron limitation and the role of Fur

et al. 2005

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Campylobacter jejuni is a zoonotic pathogen and the most common cause of bacterial foodborne diarrhoeal illness worldwide. To establish intestinal colonization prior to either a commensal or pathogenic interaction with the host, C. jejuni will encounter iron-limited niches where there is likely to be intense competition from the host and normal microbiota for iron. To gain a better understanding of iron homeostasis and the role of ferric uptake regulator (Fur) in iron acquisition in C. jejuni, a proteomic and transcriptome analysis of wild-type and fur mutant strains in iron-rich and iron-limited growth conditions was carried out. All of the proposed iron-transport systems for haemin, ferric iron and enterochelin, as well as the putative iron-transport genes p19, Cj1658, Cj0177, Cj0178 and cfrA, were expressed at higher levels in the wild-type strain under iron limitation and in the fur mutant in iron-rich conditions, suggesting that they were regulated by Fur. Genes encoding a previously uncharacterized ABC transport system (Cj1660-Cj1663) also appeared to be Fur regulated, supporting a role for these genes in iron uptake. Several promoters containing consensus Fur boxes that were identified in a previous bioinformatics search appeared not to be regulated by iron or Fur, indicating that the Fur box consensus needs experimental refinement. Binding of purified Fur to the promoters upstream of the p19, CfrA and CeuB operons was verified using an electrophoretic mobility shift assay (EMSA). These results also implicated Fur as having a role in the regulation of several genes, including fumarate hydratase, that showed decreased expression in response to iron limitation. The known PerR promoters were also derepressed in the C. jejuni Fur mutant, suggesting that they might be co-regulated in response to iron and peroxide stress. These results provide new insights into the effects of iron on metabolism and oxidative stress response as well as the regulatory role of Fur.

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Regulation of fumarase (fumB) gene expression in Escherichia coli in response to oxygen, iron and heme availability: role of the arcA, fur, and hemA gene products

Cited by 23 publications

References 0 publications

Oxygen- and Growth Rate-Dependent Regulation of Escherichia coli Fumarase (FumA, FumB, and FumC) Activity

Oxygen- and Growth Rate-Dependent Regulation of Escherichia coli Fumarase (FumA, FumB, and FumC) Activity

Comparative Genomics of 28 Salmonella enterica Isolates: Evidence for CRISPR-Mediated Adaptive Sublineage Evolution

Campylobacter jejuni gene expression in response to iron limitation and the role of Fur

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