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Genome Mining Reveals the Genus Genome mining reveals the genus Xanthomonas to be a promising reservoir for new bioactive non-ribosomally synthesized peptides Monique Royer, Ralf Koebnik, Melanie Marguerettaz, Valerie Barbe, Guillaume P. Robin, Chrystelle Brin, Sebastien Carrere, Camila Gomez, Manuela Huegelland, Ginka H. Voeller, et al. To cite this version: Monique Royer, Ralf Koebnik, Melanie Marguerettaz, Valerie Barbe, Guillaume P. Robin, et al.. Genome mining reveals the genus Xanthomonas to be a promising reservoir for new bioactive non- ribosomally synthesized peptides. BMC Genomics, BioMed Central, 2013, 14, 10.1186/1471-2164-14- 658. hal-01209938 HAL Id: hal-01209938 https://hal.archives-ouvertes.fr/hal-01209938 Submitted on 29 May 2020 HAL is a multi-disciplinary open access L’archive ouverte pluridisciplinaire HAL, est archive for the deposit and dissemination of sci- destinée au dépôt et à la diffusion de documents entific research documents, whether they are pub- scientifiques de niveau recherche, publiés ou non, lished or not. The documents may come from émanant des établissements d’enseignement et de teaching and research institutions in France or recherche français ou étrangers, des laboratoires abroad, or from public or private research centers. publics ou privés. Royer et al. BMC Genomics 2013, 14:658 http://www.biomedcentral.com/1471-2164/14/658 RESEARCH ARTICLE Open Access Genome mining reveals the genus Xanthomonas to be a promising reservoir for new bioactive non-ribosomally synthesized peptides Monique Royer1, Ralf Koebnik2, Mélanie Marguerettaz1, Valérie Barbe3, Guillaume P Robin2, Chrystelle Brin4, Sébastien Carrere5, Camila Gomez1, Manuela Hügelland6, Ginka H Völler6, Julie Noëll1, Isabelle Pieretti1, Saskia Rausch6, Valérie Verdier2, Stéphane Poussier7, Philippe Rott1, Roderich D Süssmuth6 and Stéphane Cociancich1* Abstract Background: Various bacteria can use non-ribosomal peptide synthesis (NRPS) to produce peptides or other small molecules. Conserved features within the NRPS machinery allow the type, and sometimes even the structure, of the synthesized polypeptide to be predicted. Thus, bacterial genome mining via in silico analyses of NRPS genes offers an attractive opportunity to uncover new bioactive non-ribosomally synthesized peptides. Xanthomonas is a large genus of Gram-negative bacteria that cause disease in hundreds of plant species. To date, the only known small molecule synthesized by NRPS in this genus is albicidin produced by Xanthomonas albilineans. This study aims to estimate the biosynthetic potential of Xanthomonas spp. by in silico analyses of NRPS genes with unknown function recently identified in the sequenced genomes of X. albilineans and related species of Xanthomonas. Results: We performed in silico analyses of NRPS genes present in all published genome sequences of Xanthomonas spp., as well as in unpublished draft genome sequences of Xanthomonas oryzae pv. oryzae strain BAI3 and Xanthomonas spp. strain XaS3. These two latter strains, together with X. albilineans strain GPE PC73 and X. oryzae pv. oryzae strains X8-1A and X11-5A, possess novel NRPS gene clusters and share related NRPS-associated genes such as those required for the biosynthesis of non-proteinogenic amino acids or the secretion of peptides. In silico prediction of peptide structures according to NRPS architecture suggests eight different peptides, each specific to its producing strain. Interestingly, these eight peptides cannot be assigned to any known gene cluster or related to known compounds from natural product databases. PCR screening of a collection of 94 plant pathogenic bacteria indicates that these novel NRPS gene clusters are specific to the genus Xanthomonas and are also present in Xanthomonas translucens and X. oryzae pv. oryzicola. Further genome mining revealed other novel NRPS genes specific to X. oryzae pv. oryzicola or Xanthomonas sacchari. Conclusions: This study revealed the significant potential of the genus Xanthomonas to produce new non-ribosomally synthesized peptides. Interestingly, this biosynthetic potential seems to be specific to strains of Xanthomonas associated with monocotyledonous plants, suggesting a putative involvement of non-ribosomally synthesized peptides in plant-bacteria interactions. * Correspondence: [email protected] 1CIRAD, UMR BGPI, Montpellier Cedex 5, F-34398, France Full list of author information is available at the end of the article © 2013 Royer et al.; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Royer et al. BMC Genomics 2013, 14:658 Page 2 of 19 http://www.biomedcentral.com/1471-2164/14/658 Background The A-domains are the gatekeepers of biosynthesis of Various bacteria, most prominently belonging to the orders the polypeptide due to the specificity of substrate binding Bacillales, Pseudomonadales or Actinomycetales, use non- pockets of NRPSs for their cognate substrates. Compared ribosomal peptide synthesis (NRPS) to produce peptides to the 22 proteinogenic amino acids used in ribosomal or other small molecules. These molecules exhibit broad protein synthesis, the utilization of hundreds of different structural diversity and display biological activities that non-proteinogenic amino acids has been described for range from adaptation to unfavorable environments, com- NRPS. Each substrate binding pocket of NRPSs is specific munication or competition with other microorganisms for its amino acid substrate, and predictive models based in their natural habitat, or even to action as virulence fac- on domain arrangement and on the sequence of modules tors (for review [1,2]). Non-ribosomal peptide synthetases have been deduced. The predictive power of these models (NRPSs) are megaenzymes, usually with a multimodular has been refined from sequence analyses of NRPS structure, that catalyze the non-ribosomal assembly of pep- A-domains with known specificity combined with exam- tides from proteinogenic and non-proteinogenic amino ples of crystal structures of A-domains [9-11], thus identi- acids [3,4]. A basic module consists of an adenylation do- fying amino acid residues crucial for A-domain specificity. main (A-domain) responsible for amino acid activation; a These models postulate specificity-conferring signatures peptidyl carrier protein domain (PCP-domain)—usually for NRPS A-domains consisting of ten critical amino acid adjacent to the A-domain—for thioesterification of the ac- residues putatively involved in amino acid or aryl acid sub- tivated amino acid; a condensation domain (C-domain), strate specificity. The number of NRPS modules and their which performs transpeptidation between the upstream domain organization within the enzymes determine the and downstream peptidyl and amino acyl thioesters to structure of the final peptide product. Using in silico ana- elongate the growing peptide chain. In addition to this lyses of the NRPS genes, these conserved features within basic subset of core domains, each NRPS system also has a the NRPS machinery allow prediction of the type, and chain-terminating thioesterase domain (TE-domain) that is sometimes even the structure, of the synthesized polypep- responsible for detachment of the mature polypeptide. tide. It is therefore possible to investigate the biosynthetic Typically, NRPS initiation modules lack a C-domain potential of a given bacterium by analysis of the architec- [3]. The exceptions are initiation modules of NRPS in- ture of its NRPS gene clusters. volved in biosynthesis of cyclic lipopeptides [5]. C- The transfer of a phosphopantetheinyl group to PCP- domains present in these initiation modules catalyze domains is required for posttranslational activation of N-acylation of the first amino acid with a fatty acid NRPSs. Inactive apo-NRPSs are converted to their active (with a β-hydroxy-carboxylic acid). Phylogenetic ana- holo-forms by transfer of the 4′-phosphopantetheinyl lyses of C-domains in NRPSs showed that C-domains (P-pant) moiety of coenzyme A to the sidechain hydroxyl of initiation modules, termed starter C-domains, segre- of a serine residue in the PCP-domains. The P-pant moi- gate in a separate phylogenetic clade distant from the ety serves to tether covalently the growing polypeptide C-domains of elongation NRPS modules [6]. In addition being assembled by NRPSs. Transfer of the P-pant moiety to the essential domains mentioned above (A, PCP, C and from coenzyme A to a serine residue is catalyzed by TE), optional auxiliary domains such as epimerization (E) 4′-phosphopantetheinyl transferase (PPTase). PPTases are or heterocyclization (Cy) domains can be found within involved not only in posttranslational activation of NRPS some NRPS modules. Commonly, epimerization domains but also in posttranslational activation of fatty acid and are located C-terminally of PCP-domains and perform polyketide synthases that do not contain PCP-domains epimerization of the last amino acid of the adjacent but instead have acyl carrier protein (ACP) domains. All peptidyl-thioester. Interestingly, biochemical data showed PPTases are recognized by a common signature sequence that C-domains involved in assembly of arthrofactin (V/I)G(I/V)D …x40-45… (F/W)(S/C/T)xKE(S/A)xxK, but not only catalyze transpeptidation between the up- overall sequence similarities are low [12-15]. Carrier
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