Identification of a Polyketide Synthase Required for Alternariol (AOH) and Alternariol-9-Methyl Ether (AME) Formation in Alternaria alternata

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dc.contributorVirginia Techen
dc.contributor.authorSaha, Debjanien
dc.contributor.authorFetzner,Ramonaen
dc.contributor.authorBurkhardt, Brittaen
dc.contributor.authorPodlech, Joachimen
dc.contributor.authorMetzler, Manfreden
dc.contributor.authorDang, Haen
dc.contributor.authorLawrence, Christopher B.en
dc.contributor.authorFischer, Reinharden
dc.date.accessed2014-04-08en
dc.date.accessioned2014-04-09T15:07:22Zen
dc.date.available2014-04-09T15:07:22Zen
dc.date.issued2012-07-06en
dc.description.abstractAlternaria alternata produces more than 60 secondary metabolites, among which alternariol (AOH) and alternariol-9-methyl ether (AME) are important mycotoxins. Whereas the toxicology of these two polyketide-based compounds has been studied, nothing is known about the genetics of their biosynthesis. One of the postulated core enzymes in the biosynthesisof AOH and AME is polyketide synthase (PKS). In a draft genome sequence of A. alternata we identified 10 putative PKSencoding genes. The timing of the expression of two PKS genes, pksJ and pksH, correlated with the production of AOH and AME. The PksJ and PksH proteins are predicted to be 2222 and 2821 amino acids in length, respectively. They are both iterative type I reducing polyketide synthases. PksJ harbors a peroxisomal targeting sequence at the C-terminus, suggesting that the biosynthesis occurs at least partly in these organelles. In the vicinity of pksJ we found a transcriptional regulator, altR, involved in pksJ induction and a putative methyl transferase, possibly responsible for AME formation. Downregulation of pksJ and altR caused a large decrease of alternariol formation, suggesting that PksJ is the polyketide synthase required for the postulated Claisen condensations during the biosynthesis. No other enzymes appeared to be required. PksH downregulation affected pksJ expression and thus caused an indirect effect on AOH production.en
dc.description.sponsorshipThis work was supported by the Humboldt Society and the Baden Wu¨ rttemberg Stiftung. D.S. is a Humboldt fellow. The authors thank Deutsche Forschungsgemeinschaft (DFG) and Open Access Publishing Fund of Karlsruhe Institute of Technology (KIT) for support. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.en
dc.identifier.citationSaha D, Fetzner R, Burkhardt B, Podlech J, Metzler M, et al. (2012) Identification of a Polyketide Synthase Required for Alternariol (AOH) and Alternariol-9-Methyl Ether (AME) Formation in Alternaria alternata. PLoS ONE 7(7): e40564.doi:10.1371/journal.pone.0040564en
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0040564en
dc.identifier.issn1932-6203en
dc.identifier.urihttp://hdl.handle.net/10919/47011en
dc.identifier.urlhttp://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.00405en
dc.language.isoen_USen
dc.publisherPLoS ONEen
dc.rightsIn Copyrighten
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/en
dc.subjectBiosynthesisen
dc.subjectFungal geneticsen
dc.subjectPolymerase chain reactionen
dc.subjectSeconary metabolismen
dc.subjectThin-layer chromatographyen
dc.subjectTranscription factorsen
dc.subjectTranserasesen
dc.subjectVector clonningen
dc.titleIdentification of a Polyketide Synthase Required for Alternariol (AOH) and Alternariol-9-Methyl Ether (AME) Formation in Alternaria alternataen
dc.title.serialPLoS oneen
dc.typeArticle - Refereeden

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