Fusarin C Biosynthesis in <i>Fusarium moniliforme</i> and <i>Fusarium venenatum</i>

Song, Zhiyong; Cox, Russell J.; Lazarus, Colin M.; Simpson, Thomas J.

doi:10.1002/cbic.200400138

Cited by 199 publications

(211 citation statements)

References 31 publications

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“…Microbiology 158 proteins can be grouped into three statistically supported clades, typified by the equisetin synthase of Fusarium heterosporum (EqiS; Sims et al, 2005), Gibberella moniliformis fusarinC (FusS; Song et al, 2004) and Cordyceps bassiana tenellin toxin (TenS; Eley et al, 2007)/Penicillium expansum cytochalasan synthase CheA/CytS (Schümann & Hertweck, 2007) (Fig. 4).…”

Section: P K Mukherjee and Others 160mentioning

confidence: 99%

Functional analysis of non-ribosomal peptide synthetases (NRPSs) in Trichoderma virens reveals a polyketide synthase (PKS)/NRPS hybrid enzyme involved in the induced systemic resistance response in maize

et al. 2012

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Trichoderma virens genome harbours genes encoding 22 non-ribosomal peptide synthetases (NRPSs) with at least one complete module (containing adenylation, thiolation and condensation domains) and four PKS/NRPS (polyketide synthase/NRPS) hybrid enzymes. After a primary screen for expression of these 26 genes when mycelia of T. virens are in contact with maize roots, seven genes that are upregulated were selected for further study. Using homologous recombination, loss-of-function mutants in six of these were obtained (the seventh, tex2, was acquired from our previous studies). Plant assays in a hydroponics system revealed that all seven mutants retained the ability to internally colonize maize roots. However, a mutation in one of the PKS/NRPS hybrid genes impaired the ability of T. virens to induce the defence response gene pal (phenylalanine ammonia lyase), suggesting a putative role for the associated metabolite product in induced systemic resistance. Interestingly, the mutant retained its ability to induce another defence response gene aos (allene oxide synthase). We thus provide evidence that a PKS/NRPS hybrid enzyme is involved in Trichoderma-plant interactions resulting in induction of defence responses.

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Section: P K Mukherjee and Others 160mentioning

confidence: 99%

Functional analysis of non-ribosomal peptide synthetases (NRPSs) in Trichoderma virens reveals a polyketide synthase (PKS)/NRPS hybrid enzyme involved in the induced systemic resistance response in maize

et al. 2012

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“…The F. graminearum genome encodes 15 polyketide synthases (PKS) 2 (2,3), of which FgPKS12 is the progenitor of nor-rubrofusarin/rubrofusarin/aurofusarin (4,5), FgPKS4 and FgPKS13 are the progenitors of zearalenone (1,6), FgPKS10 is the progenitor of fusarin C (7,8), and FgPKS3 is the progenitor of an uncharacterized black/purple perithecial pigment (8). PKS genes are typically found in gene clusters that comprise genes encoding transcription factor, transporters, and tailoring enzymes required for biosynthesis of the final product (1, 4 -6).…”

mentioning

confidence: 99%

Two Novel Classes of Enzymes Are Required for the Biosynthesis of Aurofusarin in Fusarium graminearum

Frandsen

Schütt

Lund

et al. 2011

Journal of Biological Chemistry

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Previous studies have reported the functional characterization of 9 out of 11 genes found in the gene cluster responsible for biosynthesis of the polyketide pigment aurofusarin in Fusarium graminearum. Here we reanalyze the function of a putative aurofusarin pump (AurT) and the two remaining orphan genes, aurZ and aurS. Targeted gene replacement of aurZ resulted in the discovery that the compound YWA1, rather than nor-rubrofusarin, is the primary product of F. graminearum polyketide synthase 12 (FgPKS12). AurZ is the first representative of a novel class of dehydratases that act on hydroxylated ␥-pyrones. Replacement of the aurS gene resulted in accumulation of rubrofusarin, an intermediate that also accumulates when the GIP1, aurF, or aurO genes in the aurofusarin cluster are deleted. Based on the shared phenotype and predicted subcellular localization, we propose that AurS is a member of an extracellular enzyme complex (GIP1-AurF-AurO-AurS) responsible for converting rubrofusarin into aurofusarin. This implies that rubrofusarin, rather than aurofusarin, is pumped across the plasma membrane. Replacement of the putative aurofusarin pump aurT increased the rubrofusarin-to-aurofusarin ratio, supporting that rubrofusarin is normally pumped across the plasma membrane. These results provide functional information on two novel classes of proteins and their contribution to polyketide pigment biosynthesis.The plant pathogenic fungus Fusarium graminearum (teleomorph Gibberella zeae) is capable of producing a plethora of secondary metabolites, many of which belong to the polyketide class of compounds, such as the mycotoxins zearalenone, fusarin C, and aurofusarin (1). The F. graminearum genome encodes 15 polyketide synthases (PKS) 2 (2, 3), of which FgPKS12 is the progenitor of nor-rubrofusarin/rubrofusarin/aurofusarin (4, 5), FgPKS4 and FgPKS13 are the progenitors of zearalenone (1, 6), FgPKS10 is the progenitor of fusarin C (7, 8), and FgPKS3 is the progenitor of an uncharacterized black/purple perithecial pigment (8). PKS genes are typically found in gene clusters that comprise genes encoding transcription factor, transporters, and tailoring enzymes required for biosynthesis of the final product (1, 4 -6). In addition to genes encoding well characterized classes of enzymes, the clusters typically also include orphan genes that encode proteins annotated as "hypothetical" or "conserved hypothetical proteins," signifying that no similarity to any previously characterized protein has been found. In the case of F. graminearum, more than half of all gene models found in the Fusarium graminearum Genome Database from the Munich Information Center for Protein Sequences (MIPS) fall into either of these two categories (9).Functional characterization of hypothetical proteins is challenging, but those belonging to secondary metabolite gene clusters provide a unique opportunity because their location suggests a function in the respective biosynthetic pathways. The PKS12 gene cluster in F. graminearum, which is responsible for biosyn...

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“…A homologous gene of fusA in F. moniliforme is responsible for the early stages of fusarin biosynthesis in F. venenatum (Song et al, 2004 The present document has been produced and adopted by the bodies identified above as author(s). This task has been carried out exclusively by the author(s) in the context of a contract between the European Food Safety Authority and the author(s), awarded following a tender procedure.…”

Section: Ergot Alkaloidsmentioning

confidence: 99%

Database on the taxonomical characterisation and potential toxigenic capacities of microorganisms used for the industrial production of food enzymes and feed additives, which do not have a recommendation for Qualified Presumption of Safety

Benito

Ibáñez

Moncho

et al. 2017

EFSA Supporting Publications

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The present work constitutes the external scientific report of the EFSA open call OC/EFSA/FEED/2015/01. The aim of the call was to provide EFSA with a database from a review on the taxonomical description and potential toxigenic capacities of microorganisms used for the industrial production of feed additives and food enzymes. The review includes microorganisms used as source of feed additives and food enzymes for which EFSA has received or can potentially receive applications for safety assessment, and which have not been recommended for Qualified Presumption of Safety status. The database also comprises the molecular taxonomical identifiers and biosynthetic pathways involved in the production of toxic compounds and the responsible genes. The main result of the project is shown as a database developed according to the EFSA data structure. The methodological aspects and the queries used in the systematic search, as well as the procedure applied for the screening of scientific documents retrieved are described in this report. Details are available in supplementary appendices.In total, 22970 scientific documents were screened in the literature search, from which 411 were initially selected for providing pertinent data for the scope of the project. From the review of the selected articles, 474 bioactive secondary metabolites were recorded and 59 compounds were further studied in order to obtain data on their toxicology and the conditions in which they are produced by the microorganisms used in industrial fermentations. The database generated in this project comprises details that characterise, when available, the production conditions, genes involved and toxicity of these 59 compounds. This provides information that can be used to establish safety measures when using potentially toxigenic microorganisms in industrial fermentations Disclaimer: The present document has been produced and adopted by the bodies identified above as author(s). This task has been carried out exclusively by the author(s) in the context of a contract between the European Food Safety Authority and the author(s), awarded following a tender procedure. The present document is published complying with the transparency principle to which the Authority is subject. It may not be considered as an output adopted by the Authority. The European Food Safety Authority reserves its rights, view and position as regards the issues addressed and the conclusions reached in the present document, without prejudice to the rights of the authors. Acknowledgements:We thank the following EFSA satff: Jaime Aguilera, Margarita Aguilera-Gómez, Jane Richardson, Mario Monguidi and Davide Gibin for their valuable help and collaboration throughout the project. We also would like to thank the members of AINIA: Sonia Porta, Lidia Tomás, Joaquin Espí and Juan Antonio Nieto for providing expertise in biotechnology and molecular biology and contributing with their efforts to achieve the goals of this project, and Violeta Gómez from the University of Navarra for her colla...

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Fusarin C Biosynthesis in Fusarium moniliforme and Fusarium venenatum

Cited by 199 publications

References 31 publications

Functional analysis of non-ribosomal peptide synthetases (NRPSs) in Trichoderma virens reveals a polyketide synthase (PKS)/NRPS hybrid enzyme involved in the induced systemic resistance response in maize

Functional analysis of non-ribosomal peptide synthetases (NRPSs) in Trichoderma virens reveals a polyketide synthase (PKS)/NRPS hybrid enzyme involved in the induced systemic resistance response in maize

Two Novel Classes of Enzymes Are Required for the Biosynthesis of Aurofusarin in Fusarium graminearum

Database on the taxonomical characterisation and potential toxigenic capacities of microorganisms used for the industrial production of food enzymes and feed additives, which do not have a recommendation for Qualified Presumption of Safety

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