HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Williams, J. S. Articles by Clarke, D. J. Search for Related Content PubMed PubMed Citation Articles by Williams, J. S. Articles by Clarke, D. J. Agricola Articles by Williams, J. S. Articles by Clarke, D. J.

The gene stlA encodes a phenylalanine ammonia-lyase that is involved in the production of a stilbene antibiotic in Photorhabdus luminescens TT01

Molecular Microbiology Laboratory, Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK

Correspondence
David J. Clarke
bssdjc{at}bath.ac.uk

Photorhabdus is a genus of Gram-negative bacteria from the family Enterobacteriaceae. Members of Photorhabdus have a complex life cycle during which the bacterium has a pathogenic interaction with insect larvae whilst also maintaining a mutualistic relationship with nematodes from the family Heterorhabditidae. During growth in the insect, Photorhabdus bacteria produce a broad-spectrum antibiotic identified as 3,5-dihydroxy-4-isopropylstilbene (ST). The biochemical pathway responsible for the production of this antibiotic has not been characterized. In this report, a mutant strain of Photorhabdus luminescens subsp. laumondii TT01, BMM901, has been isolated, by transposon mutagenesis, that is unable to produce the ST antibiotic. Using in silico studies, feeding experiments and biochemical analyses, it is shown that the gene mutated in this strain, stlA, encodes phenylalanine ammonia-lyase (PAL). PAL catalyses the non-oxidative deamination of L-phenylalanine to trans-cinnamic acid and the enzyme is ubiquitous in plants, where it is involved in the production of phenylpropanoids such as lignin and phytoalexins. However, this is the first report of PAL activity in a member of the Proteobacteria.

This article has been cited by other articles:

				S. Chalabaev, E. Turlin, S. Bay, C. Ganneau, E. Brito-Fravallo, J.-F. Charles, A. Danchin, and F. Biville Cinnamic Acid, an Autoinducer of Its Own Biosynthesis, Is Processed via Hca Enzymes in Photorhabdus luminescens Appl. Envir. Microbiol., March 15, 2008; 74(6): 1717 - 1725. [Abstract] [Full Text] [PDF]

				E. Krin, N. Chakroun, E. Turlin, A. Givaudan, F. Gaboriau, I. Bonne, J.-C. Rousselle, L. Frangeul, C. Lacroix, M.-F. Hullo, et al. Pleiotropic Role of Quorum-Sensing Autoinducer 2 in Photorhabdus luminescens. Appl. Envir. Microbiol., October 1, 2006; 72(10): 6439 - 6451. [Abstract] [Full Text] [PDF]

				M. Berner, D. Krug, C. Bihlmaier, A. Vente, R. Muller, and A. Bechthold Genes and Enzymes Involved in Caffeic Acid Biosynthesis in the Actinomycete Saccharothrix espanaensis. J. Bacteriol., April 1, 2006; 188(7): 2666 - 2673. [Abstract] [Full Text] [PDF]