This Article Full Text (PDF) Other Versions of this Article: AAC.00261-07v1 51/10/3546    most recent 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 Vassiliadis, G. Articles by Destoumieux-Garzón, D. Search for Related Content PubMed PubMed Citation Articles by Vassiliadis, G. Articles by Destoumieux-Garzón, D.

 Previous Article  |  Next Article 

Antimicrob. Agents Chemother. doi:10.1128/AAC.00261-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Insight into siderophore-peptide biosynthesis: Enterobactin is a precursor for microcin E492 post-translational modification

Chimie et Biochimie des Substances Naturelles, CNRS-Muséum National d'Histoire Naturelle, UMR 5154, CP 54, 57 rue Cuvier, 75005 Paris, France

^* To whom correspondence should be addressed. Email: peduzzi{at}mnhn.fr.

	Abstract

Microcin E492-producing bacteria secrete both unmodified and post-translationally modified microcins. The modification consists of a C-glucosylated linear trimer of N-(2,3-dihydroxybenzoyl)-L-serine, a catecholate siderophore related to salmochelins and enterobactin. We showed here that repression of enterobactin biosynthesis inhibits the acquisition of microcin E492 post-translational modification, as monitored by high-performance liquid chromatography and mass spectrometry. Furthemore, exogenous enterobactin restored the production of post-translationally modified microcin in a bacterial strain deficient in enterobactin synthesis. We thus concluded that enterobactin serves as a precursor for the synthesis of the post-translationally modified microcin and that the unmodified microcin is an incompletely processed form of the mature microcin E492. Gene disruption experiments showed that MceC and MceD, two enzymes encoded by the mceABCDEFGHIJ gene cluster, are involved in the synthesis of microcin E492 post-translational modification, as followed by mass spectrometry. Genes homologous to iroB and iroD, required for the conversion (linearization and C-glycosylation) of enterobactin into salmochelins, efficiently complemented mceC and mceD, respectively. Based on our results, a model is proposed for the biosynthesis of the mature siderophore-peptide.

This article has been cited by other articles:

• Mercado, G., Tello, M., Marin, M., Monasterio, O., Lagos, R. (2008). The Production In Vivo of Microcin E492 with Antibacterial Activity Depends on Salmochelin and EntF. J. Bacteriol. 190: 5464-5471 [Abstract] [Full Text]