Comparison of Porphyrin and Heme Biosynthesis
in Various Heterotrophic Bacteria

Philipp-Dormston, W. K.; Doss, M.

doi:10.1159/000459362

Cited by 45 publications

(41 citation statements)

References 6 publications

(8 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…2a). As expected, and in agreement with earlier observations for various other bacteria, the wild-type and mutant strains grown in the absence of ALA did not contain significantly overproduced tetrapyrroles (Doss & Philipp-Dornston, 1971;Philipp-Dornston & Doss, 1973).…”

Section: Defect In the Haem Exporter Ccmc Or The Ferrochelatase Hemh supporting

confidence: 92%

“…Porphyrinogens and porphyrins accumulated by the ccmC mutant grown in the presence and absence of ALA were determined by HPLC analysis. ALA was added to growth media to overcome the initial rate-limiting step of tetrapyrrole biosynthesis and to allow significant detectable tetrapyrrole accumulation (Doss & Philipp-Dornston, 1971;Philipp-Dornston & Doss, 1973). The data presented in Fig.…”

Section: Defect In the Haem Exporter Ccmc Or The Ferrochelatase Hemh mentioning

confidence: 99%

See 1 more Smart Citation

Co-ordination of iron acquisition, iron porphyrin chelation and iron–protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

et al. 2003

View full text Add to dashboard Cite

The cytoplasmic membrane protein CcmC is, together with other Ccm proteins, a component for the maturation of c-type cytochromes in Gram-negative bacteria. A Pseudomonas fluorescens ATCC 17400 ccmC mutant is cytochrome c-deficient and shows considerably reduced production of the two siderophores pyoverdine and quinolobactin, paralleled by a general inability to utilize various iron sources, with the exception of haem. The ccmC mutant accumulates in a 5-aminolevulinic acid-dependent synthesis a reddish, fluorescent pigment identified as protoporphyrin IX. As a consequence a visA phenotype similar to that of a ferrochelatase-deficient hemH mutant characterized by drastically reduced growth upon light exposure was observed for the ccmC mutant. The defect of iron–protoporphyrin formation was further demonstrated by the failure of ccmC cell-free proteinase K-treated extracts to stimulate the growth of a haem auxotrophic hemH indicator strain, compared to similarly prepared wild-type extracts. In addition, the ccmC mutant did not sustain hemH growth in cross-feeding experiments while the wild-type did. Significantly reduced resistance to oxidative stress mediated by haem-containing catalases was observed for the ccmC mutant. A double hemH ccmC mutant could not be obtained in the presence of external haem without the hemH gene in trans, indicating that the combination of the two mutations is lethal. It was concluded that CcmC, apart from its known function in cytochrome c biogenesis, plays a role in haem biosynthesis. A function in the regulatory co-ordination of iron acquisition via siderophores, iron insertion into porphyrin via ferrochelatase and iron–protoporphyrin export for cytochrome c formation is predicted.

show abstract

Section: Defect In the Haem Exporter Ccmc Or The Ferrochelatase Hemh supporting

confidence: 92%

Section: Defect In the Haem Exporter Ccmc Or The Ferrochelatase Hemh mentioning

confidence: 99%

Co-ordination of iron acquisition, iron porphyrin chelation and iron–protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

et al. 2003

View full text Add to dashboard Cite

show abstract

“…We attempted to overcome these putative cofactor deficiencies by adding FeCl3 and the porphyrin percursor 5-aminolevulinic acid (31) to the medium but were unsuccessful. We then considered the possibility that synthesis of siroheme from uroporphyrinogen III might be limiting for holoenzyme activity.…”

Section: Resultsmentioning

confidence: 99%

High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor

Siegel

Kredich

1991

J Bacteriol

View full text Add to dashboard Cite

The flavoprotein and hemoprotein components of Escherichia coli B NADPH-sulfite reductase are encoded by cysJ and cysl, respectively. Plasmids containing these two genes overexpressed flavoprotein catalytic activity and apohemoprotein by 13-to 35-fold, but NADPH-sulfite reductase holoenzyme activity was increased only 3-fold. Maximum overexpression of holoenzyme activity was achieved by the inclusion in such plasmids of Salmonella typhimurium cysG, which encodes a uroporphyrinogen III methyltransferase required for the synthesis of siroheme, a cofactor for the hemoprotein. Thus, cofactor deficiency, in this case siroheme, can limit overexpression of a cloned enzyme. Catalytically active holoenzyme accounted for 10% of total soluble protein in a host containing cloned cysJ, cysI, and cysG. A 5.3-kb DNA fragment containing S. typhimurium cysG was sequenced, and the open reading frame corresponding to cysG was identified by subcloning and by identifying plasmid-encoded peptides in maxicells. Comparison with the sequence reported for the E. coli cysG region (J. A. Cole, unpublished data; GenBank sequence ECONIRBC) indicates a gene order of nirB-nirC-cysG in the cloned S. typhimurium fragment. In addition, two open reading frames of unknown identity were found immediately downstream of cysG. One of these contains 11 direct repeats of 33 nucleotides each, which correspond to the consensus amino acid sequence Asp-Asp-Val-Thr-Pro-Pro-Asp-Asp-Ser-Gly-Asp.NADPH-sulfite reductase (SiR) of Escherichia coli and Salmonella typhimurium catalyzes the reduction of sulfite to sulfide and is required for synthesis of L-cysteine from inorganic sulfate (8,14). The native enzyme has a subunit structure a8,4, where a8 is a flavoprotein (SiR-FP) containing both flavin adenine dinucleotide and flavin mononucleotide and P is a hemoprotein (SiR-HP) containing an Fe4S4 center and a single molecule of siroheme (24,25,37,39). Electron flow between these cofactors proceeds from NADPH to flavin adenine dinucleotide to flavin mononucleotide in the flavoprotein, then to a closely coupled Fe4S4-siroheme center in the hemoprotein, and finally from siroheme to sulfite (38).The SiR-FP and SiR-HP components of SiR are encoded by cysJ and cysl, respectively. These genes are contiguous and together with cysH, the gene for 3'-phosphoadenosine 5'-phosphosulfate sulfotransferase, comprise an operon with the gene order promoter-cysJ-cysI-cysH (7,17,(26)(27)(28)(29). The cysJIH operon is part of the positively regulated cysteine regulon (15) and requires sulfur limitation, CysB protein, and either O-acetyl-L-serine or N-acetyl-L-serine for expression (10,11,14,28). SiR activity is also dependent on cysG, which encodes a uroporphyrinogen III methyltransferase necessary for the synthesis of siroheme (42). This gene is located more than 10 min away from cysJIH on the chromosomal map (34) and is not tightly regulated as part of the cysteine regulon (27,28). In E. coli, cysG is closely linked to nirB, the gene for another siroheme-containing enzyme, nitrite redu...

show abstract

“…The formation of 5-aminolevulinic acid (ALA), the first committed precursor of all tetrapyrroles, has been found to be the central regulatory point for tetrapyrrole formation. External factors like the oxygen and nitrate content of the environment and internal parameters like the heme content of the cell strongly influence the rate of ALA biosynthesis (13,15,17,21,28,34,35,40,50,54).Two dissimiliar routes for ALA biosynthesis are used in nature. The Shemin pathway utilizes the one-step condensation of glycine and succinyl coenzyme A by ALA synthase, and it is present in the ␣ group of the proteobacteria and in yeast and mammalian cells (13,15,40,50).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

Regulation of the hemA gene during 5-aminolevulinic acid formation in Pseudomonas aeruginosa

et al. 1995

View full text Add to dashboard Cite

The general tetrapyrrole precursor 5-aminolevulinic acid is formed in bacteria via two different biosynthetic pathways. Members of the ␣ group of the proteobacteria use 5-aminolevulinic acid synthase for the condensation of succinyl-coenzyme A and glycine, while other bacteria utilize a two-step pathway from aminoacylated tRNA Glu . The tRNA-dependent pathway, involving the enzymes glutamyl-tRNA reductase (encoded by hemA) and glutamate-1-semialdehyde-2,1-aminomutase (encoded by hemL), was demonstrated to be used by Pseudomonas aeruginosa, Pseudomonas putida, Pseudomonas stutzeri, Comamonas testosteroni, Azotobacter vinelandii, and Acinetobacter calcoaceticus. To study the regulation of the pathway, the glutamyl-tRNA reductase gene (hemA) from P. aeruginosa was cloned by complementation of an Escherichia coli hemA mutant. The hemA gene was mapped to the SpeI A fragment and the DpnIL fragment of the P. aeruginosa chromosome corresponding to min 24.1 to 26.8. The cloned hemA gene, coding for a protein of 423 amino acids with a calculated molecular mass of 46,234 Da, forms an operon with the gene for protein release factor 1 (prf1). This translational factor mediates the termination of the protein chain at the ribosome at amber and ochre codons. Since the cloned hemA gene did not possess one of the appropriate stop codons, an autoregulatory mechanism such as that postulated for the enterobacterial system was ruled out. Three open reading frames of unknown function transcribed in the opposite direction to the hemA gene were found. hemM/orf1 and orf2 were found to be homologous to open reading frames located in the 5 region of enterobacterial hemA genes. While orf2 was found to be 59% identical to its enterobacterial counterpart, hemM/orf1 showed only 23% identity. The third open reading frame (orf3), located between the hemA gene and hemM/orf1, encodes a polypeptide with homology to outer membrane proteins. Biochemical and genetic evidence which makes a direct involvement of HemM/ Orf1 in the 5-aminolevulinic acid formation of P. aeruginosa very unlikely was obtained. An increase of hemA mRNA was observed under anaerobic denitrifying conditions, while anaerobic growth utilizing the fermentative arginine deiminase pathway led to a drastic decrease of hemA transcription compared with that observed for aerobically grown P. aeruginosa. These results suggest the anaerobic induction of hemA by the presence of nitrate. Two transcription start sites were located in the 5 region of the hemA gene. Utilization of both transcription start sites was changed in a P. aeruginosa mutant missing the oxygen regulator Anr (Fnr analog), indicating the involvement of the transcription factor in hemA expression. DNA sequences homologous to one half of an Anr binding site were detected at one of the determined transcription start sites.The tetrapyrrole content of a bacterial cell varies drastically depending on the conditions of the growth environment. The formation of 5-aminolevulinic acid (ALA), the first committed precursor of all tetra...

show abstract

Comparison of Porphyrin and Heme Biosynthesis in Various Heterotrophic Bacteria

Cited by 45 publications

References 6 publications

Co-ordination of iron acquisition, iron porphyrin chelation and iron–protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

Co-ordination of iron acquisition, iron porphyrin chelation and iron–protoporphyrin export via the cytochrome c biogenesis protein CcmC in Pseudomonas fluorescens

High-level expression of Escherichia coli NADPH-sulfite reductase: requirement for a cloned cysG plasmid to overcome limiting siroheme cofactor

Regulation of the hemA gene during 5-aminolevulinic acid formation in Pseudomonas aeruginosa

Contact Info

Product

Resources

About