Identification of new, conserved, non‐ribosomal peptide synthetases from fluorescent pseudomonads involved in the biosynthesis of the siderophore pyoverdine

Summary Pyoverdines, the main siderophores of fluorescent pseudomonads, contain a peptide moiety, different for each pyoverdine, and an identical chromophore. While it has been shown that non‐ribosomal peptide synthetases (NRPSs) are involved in the biosynthesis of the peptide chain of pyoverdines,...

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Published inMolecular microbiology Vol. 45; no. 6; pp. 1673 - 1685
Main Authors Mossialos, Dimitris, Ochsner, Urs, Baysse, Christine, Chablain, Patrice, Pirnay, Jean‐Paul, Koedam, Nico, Budzikiewicz, Herbert, Fernández, Diana Uría, Schäfer, Mathias, Ravel, Jacques, Cornelis, Pierre
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Science Ltd 01.09.2002
Blackwell Publishing Ltd
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Summary:Summary Pyoverdines, the main siderophores of fluorescent pseudomonads, contain a peptide moiety, different for each pyoverdine, and an identical chromophore. While it has been shown that non‐ribosomal peptide synthetases (NRPSs) are involved in the biosynthesis of the peptide chain of pyoverdines, this was not demonstrated for the biosynthesis of the chromo‐phore part. We found that PvsA, from Pseudomonas fluorescens ATCC 17400, and PvdL (PA2424), from Pseudomonas aeruginosa are similar NRPSs and functional homologues, necessary for the production of pyoverdine. Transcriptional lacZ fusions showed that pvdL is co‐transcribed with the upstream PA2425 gene, encoding a putative thioesterase, and is iron‐regulated via PvdS. Similarly, RT‐PCR analysis revealed that expression of pvsA is repressed by iron. Analysis of the adenylation domains of PvsA, PvdL and their homologues, revealed that their N‐terminus starts with an acyl‐CoA ligase module, followed by three amino acid activation domains. Computer modelling of these domains suggests that PvsA in P. fluorescens and PvdL in P. aeruginosa are orthologues involved in the biosynthesis of the pyoverdine chromophore.
Bibliography:Present address: Imperial College of Science, Technology and Medicine, Department of Biology, SAFB, Imperial College Road, SW7 2A2 London, UK.
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ISSN:0950-382X
1365-2958
DOI:10.1046/j.1365-2958.2002.03120.x