Regulation of <i>Pseudomonas aeruginosa hemF</i> and <i>hemN</i> by the dual action of the redox response regulators Anr and Dnr

Rompf, Alexandra; Hungerer, Christoph; Hoffmann, Tamara; Lindenmeyer, Maja T.; Römling, Ute; Groß, U.; Doss, M; Arai, Hiroyuki; Igarashi, Yasuo; Jahn, Dieter

doi:10.1046/j.1365-2958.1998.00980.x

Cited by 80 publications

(92 citation statements)

References 51 publications

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“…-Surprisingly, the HEM13 gene of yeast and the hemF gene of Pseudomonas aeruginosa both encoding oxygen-dependent CPOs are drastically induced under anaerobic growth conditions (22,23). Similar findings were described for oxygen-dependent ribonucleotide reductase from E. coli (24).…”

Section: Oxygen-loaded E Coli Hemf Allows One Catalytic Turnover Undmentioning

confidence: 59%

Oxygen-dependent Coproporphyrinogen III Oxidase (HemF) from Escherichia coli Is Stimulated by Manganese

Breckau

Mahlitz

Sauerwald

et al. 2003

Journal of Biological Chemistry

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During heme biosynthesis in Escherichia coli two structurally unrelated enzymes, one oxygen-dependent (HemF) and one oxygen-independent (HemN), are able to catalyze the oxidative decarboxylation of coproporphyrinogen III to form protoporphyrinogen IX. Oxygendependent coproporphyrinogen III oxidase was produced by overexpression of the E. coli hemF in E. coli and purified to apparent homogeneity. The dimeric enzyme showed a K m value of 2.6 M for coproporphyrinogen III with a k cat value of 0.17 min ؊1 at its optimal pH of 6. HemF does not utilize protoporphyrinogen IX or coproporphyrin III as substrates and is inhibited by protoporphyrin IX. Molecular oxygen is essential for the en-

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Section: Oxygen-loaded E Coli Hemf Allows One Catalytic Turnover Undmentioning

confidence: 59%

Oxygen-dependent Coproporphyrinogen III Oxidase (HemF) from Escherichia coli Is Stimulated by Manganese

Breckau

Mahlitz

Sauerwald

et al. 2003

Journal of Biological Chemistry

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“…In addition to hcnA and PA1557, two other genes that were AlgR dependent in the transcriptional profiling analysis (Tables 2 and 4) are known to be ANR dependent. The arcDABC operon, which encodes the anaerobic arginine deiminase enzymes (22), and hemN, which encodes the oxygen-independent coproporphyrinogen III oxidase (49), are both ANR dependent. None of the conditions that we examined by transcriptional profiling revealed that anr was AlgR regulated.…”

Section: Discussionmentioning

confidence: 99%

Identification of AlgR-Regulated Genes in Pseudomonas aeruginosa by Use of Microarray Analysis

et al. 2004

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The Pseudomonas aeruginosa transcriptional regulator AlgR controls a variety of different processes, including alginate production, type IV pilus function, and virulence, indicating that AlgR plays a pivotal role in the regulation of gene expression. In order to characterize the AlgR regulon, Pseudomonas Affymetrix GeneChips were used to generate the transcriptional profiles of (i) P. aeruginosa PAO1 versus its algR mutant in mid-logarithmic phase, (ii) P. aeruginosa PAO1 versus its algR mutant in stationary growth phase, and (iii) PAO1 versus PAO1 harboring an algR overexpression plasmid. Expression analysis revealed that, during mid-logarithmic growth, AlgR activated the expression of 58 genes while it repressed the expression of 37 others, while during stationary phase, it activated expression of 45 genes and repression of 14 genes. Confirmatory experiments were performed on two genes found to be AlgR repressed (hcnA and PA1557) and one AlgR-activated operon (fimU-pilVWXY1Y2). An S1 nuclease protection assay demonstrated that AlgR repressed both known hcnA promoters in PAO1. Additionally, direct measurement of hydrogen cyanide (HCN) production showed that P. aeruginosa PAO1 produced threefold-less HCN than did its algR deletion strain. AlgR also repressed transcription of two promoters of the uncharacterized open reading frame PA1557. Further, the twitching motility defect of an algR mutant was complemented by the fimTU-pilVWXY1Y2E operon, thus identifying the AlgR-controlled genes responsible for this defect in an algR mutant. This study identified four new roles for AlgR: (i) AlgR can repress gene transcription, (ii) AlgR activates the fimTU-pilVWXY1Y2E operon, (iii) AlgR regulates HCN production, and (iv) AlgR controls transcription of the putative cbb 3 -type cytochrome PA1557.

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“…Interestingly, the authors (30) demonstrated that hemN is highly expressed in A. eutrophus cells grown anaerobically on nitrate and only weakly expressed in aerobic cells. Negative regulation of the hemN expression by oxygen was also observed in E. coli (31) and Pseudomonas aeruginosa (32). On the other hand, no obvious oxygen regulation was observed for the Bacillus subtilis hemN gene (33).…”

Section: Figmentioning

confidence: 91%

A Novel Mechanism for the Regulation of Photosynthesis Gene Expression by the TspO Outer Membrane Protein of Rhodobacter sphaeroides 2.4.1

Yeliseev

Kaplan

1999

Journal of Biological Chemistry

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A bacterial homolog of the mammalian mitochondrial benzodiazepine receptor, the tryptophan-rich sensory protein (TspO) has been previously demonstrated to negatively affect the transcriptional expression of several photosynthesis genes of Rhodobacter sphaeroides. To identify components of the signal transduction pathway from the outer membrane-localized TspO to the DNA-active transcription factor(s), we examined the involvement of TspO in the regulation of tetrapyrrole metabolism in R. sphaeroides. By analyzing the tetrapyrrole pigments accumulated by resting cell suspensions of R. sphaeroides, we demonstrated that TspO negatively regulates the activity of coproporphyrinogen III oxidase in this bacterium. hemN, encoding one of the isoenzymes of coproporphyrinogen III oxidase of R. sphaeroides, provided in trans to the wild type strain, produced a TSPO1 mutant phenotype by abolishing the negative effect of TspO on the transcription of the photosynthesis genes, crtI and puc. It is proposed that TspO, by regulating the exit of certain tetrapyrrole intermediates of the heme/bacteriochlorophyll biosynthetic pathways in R. sphaeroides in response to the availability of molecular oxygen, causes the accumulation of a biosynthetic intermediate that serves as a corepressor for both specific pigment gene transcription and the puc operon. The relationship between the bacterial TspO and the mitochondrial peripheral benzodiazepine receptor is discussed.

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Regulation of Pseudomonas aeruginosa hemF and hemN by the dual action of the redox response regulators Anr and Dnr

Cited by 80 publications

References 51 publications

Oxygen-dependent Coproporphyrinogen III Oxidase (HemF) from Escherichia coli Is Stimulated by Manganese

Oxygen-dependent Coproporphyrinogen III Oxidase (HemF) from Escherichia coli Is Stimulated by Manganese

Identification of AlgR-Regulated Genes in Pseudomonas aeruginosa by Use of Microarray Analysis

A Novel Mechanism for the Regulation of Photosynthesis Gene Expression by the TspO Outer Membrane Protein of Rhodobacter sphaeroides 2.4.1

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