Appl. Environ. Microbiol. doi:10.1128/AEM.02589-07
Copyright (c) 2008, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.
Cinnamic acid, an autoinducer of its own biosynthesis, is processed via Hca enzymes in Photorhabdus luminescens
Sabina Chalabaev,
Evelyne Turlin,
Sylvie Bay,
Christelle Ganneau,
Emma Brito-Fravallo,
Jean-François Charles,
Antoine Danchin,
and
Francis Biville*
Unité de Génétique des Génomes Bactériens, CNRS URA 2171, Institut Pasteur; Unité de Chimie Organique, CNRS URA 2128, Institut Pasteur; Unité de Génétique des Membranes Bactériennes, CNRS URA2172, Institut Pasteur, 25 rue du Dr Roux, 75724 Paris Cedex 15, France
* To whom correspondence should be addressed. Email:
fbiville{at}pasteur.fr.
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Abstract |
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Photorhabdus luminescens, an entomopathogenic bacterium and nematode symbiont, has homologues of the Hca and Mhp enzymes. In Escherichia coli, these enzymes catalyze 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 expression of the stlA gene, coding for PAL. P. luminescens releases endogenous CA into the medium at the end of exponential growth, and then consumes 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: biosynthesis of ST, and a pathway involving the Hca and Mhp enzymes.