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J. Biol. Chem., Vol. 280, Issue 11, 10403-10409, March 18, 2005

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Altering Substrate Chain Length Specificity of an Acylhomoserine Lactone Synthase in Bacterial Communication^*

Günter Brader, Solveig Sjöblom, Heidi Hyytiäinen, Karen Sims-Huopaniemi, and E. Tapio Palva

From the Viikki Biocenter, Faculty of Biosciences, Department of Biological and Environmental Sciences, Division of Genetics, P. O. Box 56, University of Helsinki, FIN-00014 Helsinki, Finland

Quorum sensing mediated by specific signal compounds (autoinducers) allows bacteria to monitor their cell density and enables a synchronized regulation of target gene sets. The best studied group of autoinducers are the acylhomoserine lactones (AHSLs), which are central to the regulation of virulence in many plant and animal pathogens. Variation of the acyl side chain of the AHSLs underlies the observed species specificity of this communication system. Here we show that even different strains of the plant pathogen Erwinia carotovora employ different dialects of this language and demonstrate the molecular basis for the acyl chain length specificity of distinct AHSL synthases. Under physiological concentrations, only the cognate AHSL with the "right" acyl chain is recognized as a signal that will switch on virulence genes. Mutagenesis of the AHSL synthase gene expI_SCC1 identified the changes M127T and F69L as sufficient to effectively alter ExpI_SCC1 (an N-3-oxohexanoyl-L-homoserine lactone producer) substrate specificity to that of an N-3-oxooctanoyl-L-homoserine lactone producer. Our data identify critical residues that define the size of the substrate-binding pocket of the AHSL synthase and will help in understanding and manipulating this bacterial language.

Received for publication, July 29, 2004 , and in revised form, December 13, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AY507108.

^* This work was supported by The Academy of Finland Grants 38033, 42180, 49905, 44252, 44883, 79776, and 202886 under the Finnish Centre of Excellence Programme 2000–2005 and grants from the Helsinki Graduate School in Biotechnology and Molecular Biology (to S. S.) and the Biocentrum Helsinki. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.com) contains additional data on acylhomoserine lactone content in supernatant and macerated tissue in the form of Supplemental Tables I and II.

To whom correspondence should be addressed. Tel.: 358-9-191-59600; Fax: 358-9-191-59076; E-mail: tapio.palva{at}helsinki.fi.

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