This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Reimmann, C. Articles by Haas, D. Search for Related Content PubMed PubMed Citation Articles by Reimmann, C. Articles by Haas, D.

 Previous Article  |  Next Article 

Journal of Bacteriology, October 2004, p. 6367-6373, Vol. 186, No. 19
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.19.6367-6373.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

PchC Thioesterase Optimizes Nonribosomal Biosynthesis of the Peptide Siderophore Pyochelin in Pseudomonas aeruginosa

Cornelia Reimmann,^1* Hiten M. Patel,² Christopher T. Walsh,² and Dieter Haas¹

Département de Microbiologie Fondamentale, Université de Lausanne, Lausanne, Switzerland,¹ Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts²

Received 6 May 2004/ Accepted 28 June 2004

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.

---

* Corresponding author. Mailing address: Département de Microbiologie Fondamentale, BÂtiment de Biologie, Université de Lausanne, CH-1015 Lausanne Dorigny, Switzerland. Phone: 41 21 6925632. Fax: 41 21 6925635. E-mail: Cornelia.Reimmann{at}imf.unil.ch.

---

Journal of Bacteriology, October 2004, p. 6367-6373, Vol. 186, No. 19
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.19.6367-6373.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Claxton, H. B., Akey, D. L., Silver, M. K., Admiraal, S. J., Smith, J. L. (2009). Structure and Functional Analysis of RifR, the Type II Thioesterase from the Rifamycin Biosynthetic Pathway. J. Biol. Chem. 284: 5021-5029 [Abstract] [Full Text]  
• Leduc, D., Battesti, A., Bouveret, E. (2007). The Hotdog Thioesterase EntH (YbdB) Plays a Role In Vivo in Optimal Enterobactin Biosynthesis by Interacting with the ArCP Domain of EntB. J. Bacteriol. 189: 7112-7126 [Abstract] [Full Text]  
• Miethke, M., Marahiel, M. A. (2007). Siderophore-Based Iron Acquisition and Pathogen Control. Microbiol. Mol. Biol. Rev. 71: 413-451 [Abstract] [Full Text]  
• Bultreys, A., Gheysen, I., de Hoffmann, E. (2006). Yersiniabactin Production by Pseudomonas syringae and Escherichia coli, and Description of a Second Yersiniabactin Locus Evolutionary Group.. Appl. Environ. Microbiol. 72: 3814-3825 [Abstract] [Full Text]