Impaired maturation of the siderophore pyoverdine chromophore in <i>Pseudomonas fluorescens</i> ATCC 17400 deficient for the cytochrome <i>c</i> biogenesis protein CcmC

Baysse, Christine; Budzikiewicz, H.; Fernández, Diana Urı́a; Cornélis, Pierre

doi:10.1016/s0014-5793(02)02915-0

Cited by 34 publications

(42 citation statements)

References 36 publications

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“…0.2 M HCl before measurement at 520 nm (Mavrodi et al, 2001;Whooley & McLoughlin, 1982). For pyoverdine measurements, supernatants were diluted 1/70 to 1/100 in 10 mM Tris/HCl pH 7.5 and excited at 400 nm with a spectrofluorimeter (Baysse et al, 2002;Mirleau et al, 2000). Lipase secretion was determined by enzymic assay according to Furutani et al (1995).…”

Section: Methodsmentioning

confidence: 99%

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

et al. 2009

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Pseudomonas aeruginosa is a ubiquitous environmental Gram-negative bacterium that is also a major opportunistic human pathogen in nosocomial infections and cystic fibrosis chronic lung infections. PhoP-PhoQ is a two-component regulatory system that has been identified as essential for virulence and cationic antimicrobial peptide resistance in several other Gram-negative bacteria. This study demonstrated that mutation of phoQ caused reduced twitching motility, biofilm formation and rapid attachment to surfaces, 2.2-fold reduced cytotoxicity to human lung epithelial cells, substantially reduced lettuce leaf virulence, and a major, 10 000-fold reduction in competitiveness in chronic rat lung infections. Microarray analysis revealed that PhoQ controlled the expression of many genes consistent with these phenotypes and with its known role in polymyxin B resistance. It was also demonstrated that PhoQ controls the expression of many genes outside the known PhoP regulon.

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Section: Methodsmentioning

confidence: 99%

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

et al. 2009

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“…Previously, we demonstrated that a P. fluorescens ATCC 17400 ccmC mutant had a greatly reduced PVD production and was impaired in PVD utilization as iron source, but not at the level of the uptake (Gaballa et al, 1996(Gaballa et al, , 1998Baysse et al, 2002). To investigate whether the absence of CcmC also affects other siderophore-mediated iron uptake systems, besides PVD, we decided to introduce the ccmC mutation into a mutant of P. fluorescens ATCC 17400 deficient for the non-ribosomal peptide synthetase PvsA, which is needed for the PVD chromophore synthesis (Mossialos et al, 2002).…”

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

confidence: 98%

“…One obvious phenotype of mutants affected in the biogenesis of c-type cytochromes is their reduced capacity to grow under conditions of iron limitation (Gaballa et al, 1996(Gaballa et al, , 1998Yeoman et al, 1997;Pearce et al, 1998;Polesky et al, 2001;Baysse et al, 2002, Viswanathan et al, 2002. The decrease in haem production can explain some of the observed phenotypes of the ccmC mutant, such as reduced production of siderophores PVD and QB.…”

Section: Absence Of Ccmc Affects the Production Of Siderophoresmentioning

confidence: 99%

“…The final step of haem biosynthesis, the insertion of iron into protoporphyrin IX (PPIX) catalysed by ferrochelatase encoded by hemH, was also proposed to be subject to regulation by iron availability (Qi & O'Brian, 2002). We isolated one mutant of P. fluorescens ATCC 17400 with a transposon insertion in the ccmC gene that showed greatly reduced production of PVD, an impaired maturation of the PVD chromophore, together with a decreased capacity to utilize this particular siderophore (Gaballa et al, 1996(Gaballa et al, , 1998Baysse et al, 2002). The product of this gene, the cytoplasmic membrane protein CcmC, is primarily involved in the biogenesis of c-type cytochromes (Thöny-Meyer, 1997; Kranz et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

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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

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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.

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“…Genes and enzymes required for pyoverdine synthesis in strain PAO, which secretes type I pyoverdine, have been characterized experimentally (1,4,12,15,16,21,23,31,34,35). This has revealed a biosynthetic pathway in which a pyoverdine precursor is assembled by nonribosomal peptide synthetases (NRPSs), with other enzymes providing the unusual amino acid substrates for the NRPSs and modifying the precursor peptide to yield the mature pyoverdine.…”

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Characterization of a Gene Encoding an Acetylase Required for Pyoverdine Synthesis in Pseudomonas aeruginosa

et al. 2006

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Strains of Pseudomonas aeruginosa secrete one of three pyoverdine siderophores (types I to III). We have characterized a gene, pvdY II (for the pvdY gene present in type II P. aeruginosa strains), that is only present in strains that make type II pyoverdine. A mutation in pvdY II prevented pyoverdine synthesis. Bioinformatic, genetic, and biochemical approaches indicate that the PvdYII enzyme catalyzes acetylation of hydroxyornithine. Expression of pvdY II is repressed by the presence of iron and upregulated by the presence of type II pyoverdine. Characterization of pvdY II provides insights into the molecular basis for production of different pyoverdines by different strains of P. aeruginosa.Pyoverdines are siderophores that are secreted by fluorescent pseudomonads and are efficient iron-scavenging compounds (6, 19). Over 50 pyoverdines are known, and all of these contain a dihydroxyquinoline-type chromophore; this is attached to a strain-specific peptide that contains unusual amino acids, such as D-isomers and amino acids that are not usually found in biomolecules, and an acyl group that varies depending on the growth conditions (Fig. 1). Ferri-pyoverdine complexes are recognized by receptor proteins located at the surfaces of the cells, and the iron is taken up by the bacteria in an energy-dependent process (reviewed in reference 27). Pyoverdines contribute to the ability of P. aeruginosa to cause infection (17, 32).Strains of P. aeruginosa secrete one of three pyoverdines (types I to III) (18). Genes and enzymes required for pyoverdine synthesis in strain PAO, which secretes type I pyoverdine, have been characterized experimentally (1,4,12,15,16,21,23,31,34,35). This has revealed a biosynthetic pathway in which a pyoverdine precursor is assembled by nonribosomal peptide synthetases (NRPSs), with other enzymes providing the unusual amino acid substrates for the NRPSs and modifying the precursor peptide to yield the mature pyoverdine. Genomic analyses imply that the pathway of synthesis is similar in outline in other Pseudomonas species (25), and this is supported by experimental evidence (2, 21, 24). Pyoverdine synthesis has not been studied experimentally in strains of P. aeruginosa other than PAO1. However, recent genomic analysis shows that strains that make different pyoverdines share many pyoverdine synthesis genes with strain PAO, but they contain additional genes that are not present in strain PAO and are proposed to be required for pyoverdine synthesis (29).In strain PAO, the pvdS gene is adjacent to a gene, pvdY, that is of unknown function, although a mutation in pvdY resulted in reduced pyoverdine synthesis (23). pvdY is also adjacent to pvdX (Fig. 2), a gene of unknown function. The same arrangement of genes has been demonstrated in strains of P. aeruginosa that make other pyoverdines (29). In strains that make type II pyoverdine, the pvdY gene (unlike the pvdS and pvdX genes) has very little sequence similarity to the pvdY gene in strains that make type I or type III pyoverdines, and it is not al...

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Impaired maturation of the siderophore pyoverdine chromophore in Pseudomonas fluorescens ATCC 17400 deficient for the cytochrome c biogenesis protein CcmC

Cited by 34 publications

References 36 publications

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

The sensor kinase PhoQ mediates virulence in Pseudomonas aeruginosa

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

Characterization of a Gene Encoding an Acetylase Required for Pyoverdine Synthesis in Pseudomonas aeruginosa

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