PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa.

Détails

ID Serval
serval:BIB_330B15D4D751
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
PchC thioesterase optimizes nonribosomal biosynthesis of the peptide siderophore pyochelin in Pseudomonas aeruginosa.
Périodique
Journal of Bacteriology
Auteur(s)
Reimmann C., Patel H.M., Walsh C.T., Haas D.
ISSN
0021-9193[print], 0021-9193[linking]
Statut éditorial
Publié
Date de publication
2004
Volume
186
Numéro
19
Pages
6367-6373
Langue
anglais
Résumé
In Pseudomonas aeruginosa, the antibiotic dihydroaeruginoate (Dha) and the siderophore pyochelin are produced from salicylate and cysteine by a thiotemplate mechanism involving the peptide synthetases PchE and PchF. A thioesterase encoded by the pchC gene was found to be necessary for maximal production of both Dha and pyochelin, but it was not required for Dha release from PchE and could not replace the thioesterase function specified by the C-terminal domain of PchF. In vitro, 2-aminobutyrate, a cysteine analog, was adenylated by purified PchE and PchF proteins. In vivo, this analog strongly interfered with Dha and pyochelin formation in a pchC deletion mutant but affected production of these metabolites only slightly in the wild type. Exogenously supplied cysteine overcame the negative effect of a pchC mutation to a large extent, whereas addition of salicylate did not. These data are in agreement with a role for PchC as an editing enzyme that removes wrongly charged molecules from the peptidyl carrier protein domains of PchE and PchF.
Mots-clé
Aminobutyric Acids/pharmacology, Bacterial Proteins/physiology, Cysteine/pharmacology, Phenols/metabolism, Pseudomonas aeruginosa/metabolism, Thiazoles
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 15:00
Dernière modification de la notice
20/08/2019 14:18
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