AEM Tips for Better Browsing
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
AEM.02589-07v1
74/6/1717    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Google Scholar
Right arrow Articles by Chalabaev, S.
Right arrow Articles by Biville, F.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chalabaev, S.
Right arrow Articles by Biville, F.
Agricola
Right arrow Articles by Chalabaev, S.
Right arrow Articles by Biville, F.
Applied and Environmental Microbiology, March 2008, p. 1717-1725, Vol. 74, No. 6
0099-2240/08/$08.00+0     doi:10.1128/AEM.02589-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Cinnamic Acid, an Autoinducer of Its Own Biosynthesis, Is Processed via Hca Enzymes in Photorhabdus luminescens{triangledown}

Sabina Chalabaev,1 Evelyne Turlin,1 Sylvie Bay,2 Christelle Ganneau,2 Emma Brito-Fravallo,1 Jean-François Charles,1 Antoine Danchin,1 and Francis Biville3*

Unité de Génétique des Génomes Bactériens, CNRS URA 2171, Institut Pasteur,1 Unité de Chimie Organique, CNRS URA 2128, Institut Pasteur,2 Unité de Génétique des Membranes Bactériennes, CNRS URA 2172, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris Cedex 15, France3

Received 16 November 2007/ Accepted 19 January 2008

Photorhabdus luminescens, an entomopathogenic bacterium and nematode symbiont, has homologues of the Hca and Mhp enzymes. In Escherichia coli, these enzymes catalyze the degradation of the aromatic compounds 3-phenylpropionate (3PP) and cinnamic acid (CA) and allow the use of 3PP as sole carbon source. P. luminescens is not able to use 3PP and CA as sole carbon sources but can degrade them. Hca dioxygenase is involved in this degradation pathway. P. luminescens synthesizes CA from phenylalanine via a phenylalanine ammonia-lyase (PAL) and degrades it via the not-yet-characterized biosynthetic pathway of 3,5-dihydroxy-4-isopropylstilbene (ST) antibiotic. CA induces its own synthesis by enhancing the expression of the stlA gene that codes for PAL. P. luminescens bacteria release endogenous CA into the medium at the end of exponential growth and then consume it. Hca dioxygenase is involved in the consumption of endogenous CA but is not required for ST production. This suggests that CA is consumed via at least two separate pathways in P. luminescens: the biosynthesis of ST and a pathway involving the Hca and Mhp enzymes.

* Corresponding author. Mailing address: Unité de Génétique des Membranes Bactériennes, CNRS URA 2172, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris Cedex 15, France. Phone: 33 1 40 61 32 77. Fax: 33 1 45 68 89 38. E-mail: fbiville{at}pasteur.fr

{triangledown} Published ahead of print on 1 February 2008.

Applied and Environmental Microbiology, March 2008, p. 1717-1725, Vol. 74, No. 6
0099-2240/08/$08.00+0     doi:10.1128/AEM.02589-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Microbiol. Mol. Biol. Rev. Eukaryot. Cell All ASM Journals

Copyright © 2008 by the American Society for Microbiology. All rights reserved.