The
            <i>pvc</i>
            Gene Cluster of
            <i>Pseudomonas aeruginosa</i>
            : Role in Synthesis of the Pyoverdine Chromophore and Regulation by PtxR and PvdS

Stintzi, Alain; Johnson, Zaiga; Stonehouse, Martin; Ochsner, Urs A.; Meyer, Jean‐Marie; Vasil, Michael L.; Poole, Keith

doi:10.1128/jb.181.13.4118-4124.1999

Cited by 98 publications

(65 citation statements)

References 45 publications

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“…PvcA and PvcB are required for synthesis of pyoverdine chromophore, they serve as signalling molecules controlling gene expression inside the cell and have been reported to be induced in biofilm and regulated by iron Significantly differentially regulated genes are marked by an asterisk. **P < 0.001. concentrations available (Stintzi et al, 1999;Hindre et al, 2008; Table 3). Thus the general transcriptional response of L. pneumophila to oxidative stress leads to the induction of two alkyl-peroxidases and iron related genes.…”

Section: Kaic Influences the Expression Of The Alkyl-peroxidases Ahpcmentioning

confidence: 99%

The Legionella pneumophila kai operon is implicated in stress response and confers fitness in competitive environments

Loza-Correa

Sahr

Rolando

et al. 2013

Environmental Microbiology

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Summary Legionella pneumophila uses aquatic protozoa as replication niche and protection from harsh environments. Although L. pneumophila is not known to have a circadian clock, it encodes homologues of the KaiBC proteins of Cyanobacteria that regulate circadian gene expression. We show that L. pneumophila kaiB, kaiC and the downstream gene lpp1114, are transcribed as a unit under the control of the stress sigma factor RpoS. KaiC and KaiB of L. pneumophila do not interact as evidenced by yeast and bacterial two-hybrid analyses. Fusion of the C-terminal residues of cyanobacterial KaiB to Legionella KaiB restores their interaction. In contrast, KaiC of L. pneumophila conserved autophosphorylation activity, but KaiB does not trigger the dephosphorylation of KaiC like in Cyanobacteria. The crystal structure of L. pneumophila KaiB suggests that it is an oxidoreductase-like protein with a typical thioredoxin fold. Indeed, mutant analyses revealed that the kai operon-encoded proteins increase fitness of L. pneumophila in competitive environments, and confer higher resistance to oxidative and sodium stress. The phylogenetic analysis indicates that L. pneumophila KaiBC resemble Synechosystis KaiC2B2 and not circadian KaiB1C1. Thus, the L. pneumophila Kai proteins do not encode a circadian clock, but enhance stress resistance and adaption to changes in the environments.

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Section: Kaic Influences the Expression Of The Alkyl-peroxidases Ahpcmentioning

confidence: 99%

The Legionella pneumophila kai operon is implicated in stress response and confers fitness in competitive environments

Loza-Correa

Sahr

Rolando

et al. 2013

Environmental Microbiology

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“…It has been demonstrated that pyoverdine is synthesized by a non-ribosomal mechanism, and is assembled by a series of enzymes including the peptide synthetase PvdD [3]. In P. aeruginosa PAO chromosome, genes implicated in synthesis of pyoverdine have been mapped at regions 23 and 47 min [5], and recently the pvc cluster localized at 66^70 min was described [6,7]. We present evidence that three open reading frames (ORFs) upstream of pvdD, called pvdIJK, form a putative cluster with pvdD and are implicated in pyoverdine biosynthesis.…”

Section: Introductionmentioning

confidence: 99%

Genomics of the 35-kb pvd locus and analysis of novel pvdIJK genes implicated in pyoverdine biosynthesis in Pseudomonas aeruginosa

Lehoux¹

2000

FEMS Microbiology Letters

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Novel putative pyoverdine synthetase pvdIJK genes were found upstream of pvdD in the 6.2-Mb chromosome of Pseudomonas aeruginosa strain PAO1. These genes formed a locus implicated in pyoverdine biosynthesis. Sequence analysis showed that the product of these genes shared 43%, 60% and 57% identity with PvdD. PvdIJK are thought to be implicated in synthesis of pyoverdine, a siderophore chelating Fe 3 . A pvdI mutant was obtained by gene disruption mutagenesis and confirmed by Southern hybridization. The pvdI mutant produced gave no significant growth on solid media supplemented with the iron chelator 2,2-dipyridyl; while the PvdI 3 phenotype abolished pyoverdine fluorescence. The role of PvdI in pathogenicity was tested by measuring the in vivo growth of P. aeruginosa wild-type and mutant strains in a chronic lung infection rat model, and by measuring the competitive infectivity index into a neutropenic mice model. The data obtained confirmed the importance of PvdI in virulence and iron uptake. ß 2000 Published by Elsevier Science B.V. on behalf of the Federation of European Microbiological Societies.

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“…The pyoverdine-reduced phenotype of the ferrochelatase vhemH mutant suggests that PPIX accumulation, or lack of heme, or both, are directly responsible for the inhibition of siderophore production. The genes for the biosynthesis of the pyoverdine chromophore have been identi¢ed [7,8]. They include one oxygen- Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The apparent molecular mass of the ferrochelatase from P. £uorescens was estimated by comparison with the bench mark protein ladder (Life Technologies). ase and one hydroxylase present in the cytoplasm, and one di-heme cytochrome c4 in the periplasm [8]. A shortage of heme could therefore cause a slow-down of the chromophore biosynthesis [8].…”

Section: Discussionmentioning

confidence: 99%

“…The peptide chain comprises unusual amino acids, such as N 5 -hydroxyornithine or N 5 -formyl-N 5 -hydroxyornithine [4]. Genes potentially involved in the synthesis of the pyoverdine chromophore in P. aeruginosa (pvcABCD) have been identi¢ed [7,8]. Also needed for the biosynthesis of pyoverdine, are pvdA [9] that encodes an L-ornithine N 5 -oxygenase, and the recently described pvdF gene that codes for a transformylase [10].…”

Section: Introductionmentioning

confidence: 99%

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Impact of mutations in hemA and hemH genes on pyoverdine production by Pseudomonas fluorescens ATCC17400

Baysse

2001

FEMS Microbiology Letters

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A Pseudomonas fluorescens Tn5 mutant, with decreased production of the siderophore pyoverdine, was obtained, with the transposon inserted in the hemA gene coding for glutamyl tRNA reductase, the enzyme that catalyzes the first step of heme biosynthesis. Since this mutant was leaky, a second round of transposition was needed to obtain a second mutant completely auxotrophic for the heme precursor Naminolevulinate (ALA). Pyoverdine production by this mutant is ALA-dependent at concentrations above those needed to sustain growth. A transposon mutant in the hemH gene that encodes the enzyme ferrochelatase showing a characteristic red fluorescence upon UV exposure as a result of porphyrins accumulation, was obtained by selecting transconjugants on LB medium containing hemin. The vhemH mutant was characterized and the corresponding hemH gene sequenced. Antibodies against P. fluorescens HemH detected the protein both in soluble and membrane fractions of the wild-type and confirmed the absence of the enzyme in the mutant. The vhemH mutant failed to produce pyoverdine, but the production of the siderophore was restored by introduction of the Pseudomonas aeruginosa hemH gene in trans. These results indicate that de novo heme biosynthesis is needed for a normal level of siderophore pyoverdine production. ß

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The pvc Gene Cluster of Pseudomonas aeruginosa : Role in Synthesis of the Pyoverdine Chromophore and Regulation by PtxR and PvdS

Cited by 98 publications

References 45 publications

The Legionella pneumophila kai operon is implicated in stress response and confers fitness in competitive environments

The Legionella pneumophila kai operon is implicated in stress response and confers fitness in competitive environments

Genomics of the 35-kb pvd locus and analysis of novel pvdIJK genes implicated in pyoverdine biosynthesis in Pseudomonas aeruginosa

Impact of mutations in hemA and hemH genes on pyoverdine production by Pseudomonas fluorescens ATCC17400

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