scholarly journals Involvement of a Natural Fusion of a Cytochrome P450 and a Hydrolase in Mycophenolic Acid Biosynthesis

2012 ◽  
Vol 78 (14) ◽  
pp. 4908-4913 ◽  
Author(s):  
Bjarne Gram Hansen ◽  
Ewelina Mnich ◽  
Kristian Fog Nielsen ◽  
Jakob Blæsbjerg Nielsen ◽  
Morten Thrane Nielsen ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Gene Cluster ◽  
Mycophenolic Acid ◽  
Polyketide Synthase ◽  
Fusion Gene ◽  
Bioinformatic Analysis ◽  
Terminal Region ◽  
Ring Closure ◽  
Content Type ◽  
Penicillium Brevicompactum

ABSTRACTMycophenolic acid (MPA) is a fungal secondary metabolite and the active component in several immunosuppressive pharmaceuticals. The gene cluster coding for the MPA biosynthetic pathway has recently been discovered inPenicillium brevicompactum, demonstrating that the first step is catalyzed by MpaC, a polyketide synthase producing 5-methylorsellinic acid (5-MOA). However, the biochemical role of the enzymes encoded by the remaining genes in the MPA gene cluster is still unknown. Based on bioinformatic analysis of the MPA gene cluster, we hypothesized that the step following 5-MOA production in the pathway is carried out by a natural fusion enzyme MpaDE, consisting of a cytochrome P450 (MpaD) in the N-terminal region and a hydrolase (MpaE) in the C-terminal region. We verified that the fusion gene is indeed expressed inP. brevicompactumby obtaining full-length sequence of thempaDEcDNA prepared from the extracted RNA. Heterologous coexpression ofmpaCand the fusion genempaDEin the MPA-nonproducerAspergillus nidulansresulted in the production of 5,7-dihydroxy-4-methylphthalide (DHMP), the second intermediate in MPA biosynthesis. Analysis of the strain coexpressingmpaCand thempaDpart ofmpaDEshows that the P450 catalyzes hydroxylation of 5-MOA to 4,6-dihydroxy-2-(hydroxymethyl)-3-methylbenzoic acid (DHMB). DHMB is then converted to DHMP, and our results suggest that the hydrolase domain aids this second step by acting as a lactone synthase that catalyzes the ring closure. Overall, the chimeric enzyme MpaDE provides insight into the genetic organization of the MPA biosynthesis pathway.

scholarly journals Molecular Basis for Mycophenolic Acid Biosynthesis in Penicillium brevicompactum

2011 ◽  
Vol 77 (9) ◽  
pp. 3035-3043 ◽  
Author(s):  
Torsten Bak Regueira ◽  
Kanchana Rueksomtawin Kildegaard ◽  
Bjarne Gram Hansen ◽  
Uffe H. Mortensen ◽  
Christian Hertweck ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Mycophenolic Acid ◽  
Molecular Basis ◽  
Polyketide Synthase ◽  
Functional Characterization ◽  
Gene Encoding ◽  
Biosynthesis Gene Cluster ◽  
Content Type ◽  
Polyketide Synthase Gene ◽  
Penicillium Brevicompactum

ABSTRACTMycophenolic acid (MPA) is the active ingredient in the increasingly important immunosuppressive pharmaceuticals CellCept (Roche) and Myfortic (Novartis). Despite the long history of MPA, the molecular basis for its biosynthesis has remained enigmatic. Here we report the discovery of a polyketide synthase (PKS), MpaC, which we successfully characterized and identified as responsible for MPA production inPenicillium brevicompactum. mpaCresides in what most likely is a 25-kb gene cluster in the genome ofPenicillium brevicompactum. The gene cluster was successfully localized by targeting putative resistance genes, in this case an additional copy of the gene encoding IMP dehydrogenase (IMPDH). We report the cloning, sequencing, and the functional characterization of the MPA biosynthesis gene cluster by deletion of the polyketide synthase genempaCofP. brevicompactumand bioinformatic analyses. As expected, the gene deletion completely abolished MPA production as well as production of several other metabolites derived from the MPA biosynthesis pathway ofP. brevicompactum. Our work sets the stage for engineering the production of MPA and analogues through metabolic engineering.

scholarly journals Versatile Enzyme Expression and Characterization System for Aspergillus nidulans, with the Penicillium brevicompactum Polyketide Synthase Gene from the Mycophenolic Acid Gene Cluster as a Test Case

2011 ◽  
Vol 77 (9) ◽  
pp. 3044-3051 ◽  
Author(s):  
Bjarne G. Hansen ◽  
Bo Salomonsen ◽  
Morten T. Nielsen ◽  
Jakob B. Nielsen ◽  
Niels B. Hansen ◽  
...  
Keyword(s):  
Functional Genomics ◽  
Aspergillus Nidulans ◽  
Filamentous Fungi ◽  
Mycophenolic Acid ◽  
Polyketide Synthase ◽  
Test Case ◽  
Content Type ◽  
Genomic Location ◽  
Polyketide Synthase Gene ◽  
Penicillium Brevicompactum

ABSTRACTAssigning functions to newly discovered genes constitutes one of the major challenges en route to fully exploiting the data becoming available from the genome sequencing initiatives. Heterologous expression in an appropriate host is central in functional genomics studies. In this context, filamentous fungi offer many advantages over bacterial and yeast systems. To facilitate the use of filamentous fungi in functional genomics, we present a versatile cloning system that allows a gene of interest to be expressed from a defined genomic location ofAspergillus nidulans. By a single USER cloning step, genes are easily inserted into a combined targeting-expression cassette ready for rapid integration and analysis. The system comprises a vector set that allows genes to be expressed either from the constitutive PgpdA promoter or from the inducible PalcA promoter. Moreover, by using the vector set, protein variants can easily be made and expressed from the same locus, which is mandatory for proper comparative analyses. Lastly, all individual elements of the vectors can easily be substituted for other similar elements, ensuring the flexibility of the system. We have demonstrated the potential of the system by transferring the 7,745-bp largempaCgene fromPenicillium brevicompactumtoA. nidulans. In parallel, we produced defined mutant derivatives ofmpaC, and the combined analysis ofA. nidulansstrains expressingmpaCor mutatedmpaCgenes unequivocally demonstrated thatmpaCindeed encodes a polyketide synthase that produces the first intermediate in the production of the medically important immunosuppressant mycophenolic acid.

scholarly journals Biosynthesis of Fusarubins Accounts for Pigmentation of Fusarium fujikuroi Perithecia

2012 ◽  
Vol 78 (12) ◽  
pp. 4468-4480 ◽  
Author(s):  
Lena Studt ◽  
Philipp Wiemann ◽  
Karin Kleigrewe ◽  
Hans-Ulrich Humpf ◽  
Bettina Tudzynski
Keyword(s):  
Secondary Metabolites ◽  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Polyketide Synthase ◽  
Biological Function ◽  
Fusarium Fujikuroi ◽  
Diverse Group ◽  
Fruiting Bodies ◽  
Content Type ◽  
Encoding Gene

ABSTRACTFusarium fujikuroiproduces a variety of secondary metabolites, of which polyketides form the most diverse group. Among these are the highly pigmented naphthoquinones, which have been shown to possess different functional properties for the fungus. A group of naphthoquinones, polyketides related to fusarubin, were identified inFusariumspp. more than 60 years ago, but neither the genes responsible for their formation nor their biological function has been discovered to date. In addition, although it is known that the sexual fruiting bodies in which the progeny of the fungus develops are darkly colored by a polyketide synthase (PKS)-derived pigment, the structure of this pigment has never been elucidated. Here we present data that link the fusarubin-type polyketides to a defined gene cluster, which we designatefsr, and demonstrate that the fusarubins are the pigments responsible for the coloration of the perithecia. We studied their regulation and the function of the single genes within the cluster by a combination of gene replacements and overexpression of the PKS-encoding gene, and we present a model for the biosynthetic pathway of the fusarubins based on these data.

scholarly journals Biosynthesis of a Complex Yersiniabactin-Like Natural Product via themicLocus in Phytopathogen Ralstonia solanacearum

2011 ◽  
Vol 77 (17) ◽  
pp. 6117-6124 ◽  
Author(s):  
Martin F. Kreutzer ◽  
Hirokazu Kage ◽  
Peter Gebhardt ◽  
Barbara Wackler ◽  
Hans P. Saluz ◽  
...  
Keyword(s):  
Natural Product ◽  
Gene Cluster ◽  
Ralstonia Solanacearum ◽  
Insertional Mutagenesis ◽  
Polyketide Synthase ◽  
Genome Mining ◽  
Content Type ◽  
A Genome ◽  
Iron Deficient ◽  
Peptide Synthetase

ABSTRACTA genome mining study in the plant pathogenic bacteriumRalstonia solanacearumGMI1000 unveiled a polyketide synthase/nonribosomal peptide synthetase gene cluster putatively involved in siderophore biosynthesis. Insertional mutagenesis confirmed the respective locus to be operational under iron-deficient conditions and spurred the isolation of the associated natural product. Bioinformatic analyses of the gene cluster facilitated the structural characterization of this compound, which was subsequently identified as the antimycoplasma agent micacocidin. The metal-chelating properties of micacocidin were evaluated in competition experiments, and the cellular uptake of gallium-micacocidin complexes was demonstrated inR. solanacearumGMI1000, indicating a possible siderophore role. Comparative genomics revealed a conservation of the micacocidin gene cluster in defined, but globally dispersed phylotypes ofR. solanacearum.

scholarly journals Comparative Phylogenomic Analysis of Cytochrome P450 Monooxygenases From Fusarium Species

2021 ◽  
Author(s):  
Wadzani Palnam Dauda ◽  
Elkanah Glen ◽  
Peter Abraham ◽  
Charles Oluwaseun Adetunji ◽  
Daji Morumda ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Gene Cluster ◽  
Polyketide Synthase ◽  
Fusarium Species ◽  
Pathogenic Fungi ◽  
Plant Diseases ◽  
Biological Research ◽  
Cytochrome P450 Monooxygenases ◽  
Phylogenomic Analysis ◽  
P450 Monooxygenases

Abstract Cytochrome P450s (P450s) are a unique multifamily class of enzymes that possess the capability to exhibit catalytic versatility in several biochemical reactions which entails metabolite biosynthesis, primary and secondary metabolism. Fusarium spp. is an important microorganism with many members known to produce secondary metabolites that cause plant diseases and mycotoxicoses in animals and humans. In this present study, from the initially screened 4,579 proteins, we elucidated the nature of abundance, evolutionary relationships, classification and cellular location of 320 cytochrome P450 from 17 phytopathogenic members of Fusarium species. The total CYPs protein sequences were phylogenetically grouped into seventeen (17) clades. Eighty-six (86) CYPs families and forty-eight (48) clans were identified. Twenty-seven (27) families were each found in only one species. The CYPs were found to be majorly localized in the endoplasmic reticulum. The non-ribosomal peptide synthetase-like (NRPS-like) gene cluster was the predominant secondary metabolic-related gene cluster across all the seventeen selected Fusarium species except in F. cucurbiticola and F. solani, where PolyKetide Synthase (PKS) was the most prevalent. The presence of numerous families and clans as observed in in this study shows the expansions of the CYPs families across Fusarium species, this CYPs family and clan expansion is often associated with the evolvement of several fungal traits that include their pathogenicity adaptation to survive on an extensive range of toxic substrates. Identification of P450 proteins in these pathogenic fungi provides fundamental information for further basic and applied biological research into the physiological and toxigenic roles of P450s in Fusarium species.

scholarly journals Genome-Based Cluster Deletion Reveals an Endocrocin Biosynthetic Pathway in Aspergillus fumigatus

2012 ◽  
Vol 78 (12) ◽  
pp. 4117-4125 ◽  
Author(s):  
Fang Yun Lim ◽  
Yanpeng Hou ◽  
Yiming Chen ◽  
Jee-Hwan Oh ◽  
Inhyung Lee ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Gene Cluster ◽  
Biosynthetic Pathway ◽  
Polyketide Synthase ◽  
Wild Type Strain ◽  
Global Regulator ◽  
Content Type ◽  
In The Wild ◽  
Secondary Metabolite Gene Cluster

ABSTRACTEndocrocin is a simple anthraquinone frequently identified in extracts of numerous fungi. Several biosynthetic schemes for endocrocin synthesis have been hypothesized, but to date, no dedicated secondary metabolite gene cluster that produces this polyketide as its major metabolite has been identified. Here we describe our biosynthetic and regulatory characterization of the endocrocin gene cluster inAspergillus fumigatus. This is the first report of this anthraquinone in this species. The biosynthetic genes required for endocrocin production are regulated by the global regulator of secondary metabolism, LaeA, and encode an iterative nonreducing polyketide synthase (encA), a physically discrete metallo-β-lactamase type thioesterase (encB), and a monooxygenase (encC). Interestingly, the deletion of a gene immediately adjacent toencC, termedencDand encoding a putative 2-oxoglutarate-Fe(II) type oxidoreductase, resulted in higher levels of endocrocin production than in the wild-type strain, whereas overexpression ofencDeliminated endocrocin accumulation. We found that overexpression of theencAtranscript resulted in higher transcript levels ofencA-Dand higher production of endocrocin. We discuss a model of theenccluster as one evolutionary origin of fungal anthraquinones derived from a nonreducing polyketide synthase and a discrete metallo-β-lactamase-type thioesterase.

scholarly journals 3,6-Dichlorosalicylate Catabolism Is Initiated by the DsmABC Cytochrome P450 Monooxygenase System inRhizorhabdus dicambivoransNdbn-20

2017 ◽  
Vol 84 (4) ◽  
Author(s):  
Na Li ◽  
Li Yao ◽  
Qin He ◽  
Jiguo Qiu ◽  
Dan Cheng ◽  
...  
Keyword(s):  
Cytochrome P450 ◽  
Bioinformatic Analysis ◽  
Heme Iron ◽  
Cytochrome P450 Monooxygenase ◽  
Monooxygenase System ◽  
Catabolic Pathway ◽  
P450 Monooxygenase ◽  
Content Type ◽  
Promising Target

ABSTRACTThe degradation of the herbicide dicamba is initiated by demethylation to form 3,6-dichlorosalicylate (3,6-DCSA) inRhizorhabdusdicambivoransNdbn-20. In the present study, a 3,6-DCSA degradation-deficient mutant, Ndbn-20m, was screened. A cluster,dsmR1DABCEFGR2, was lost in this mutant. The cluster consisted of nine genes, all of which were apparently induced by 3,6-DCSA. DsmA shared 30 to 36% identity with the monooxygenase components of reported three-component cytochrome P450 systems and formed a monophyletic branch in the phylogenetic tree. DsmB and DsmC were most closely related to the reported [2Fe-2S] ferredoxin and ferredoxin reductase, respectively. The disruption ofdsmAin strain Ndbn-20 resulted in inactive 3,6-DCSA degradation. WhendsmABC, but notdsmAalone, was introduced into mutant Ndbn-20m andSphingobium quisquiliarumDC-2 (which is unable to degrade salicylate and its derivatives), they acquired the ability to hydroxylate 3,6-DCSA. Single-crystal X-ray diffraction demonstrated that the DsmABC-catalyzed hydroxylation occurred at the C-5 position of 3,6-DCSA, generating 3,6-dichlorogentisate (3,6-DCGA). In addition, DsmD shared 51% identity with GtdA (a gentisate and 3,6-DCGA 1,2-dioxygenase) fromSphingomonassp. strain RW5. However, unlike GtdA, the purified DsmD catalyzed the cleavage of gentisate and 3-chlorogentisate but not 6-chlorogentisate or 3,6-DCGAin vitro. Based on the bioinformatic analysis and gene function studies, a possible catabolic pathway of dicamba inR. dicambivoransNdbn-20 was proposed.IMPORTANCEDicamba is widely used to control a variety of broadleaf weeds and is a promising target herbicide for the engineering of herbicide-resistant crops. The catabolism of dicamba has thus received increasing attention. Bacteria mineralize dicamba initially via demethylation, generating 3,6-dichlorosalicylate. However, the catabolism of 3,6-dichlorosalicylate remains unknown. In this study, we cloned a gene cluster,dsmR1DABCEFGR2, involved in 3,6-dichlorosalicylate degradation fromR. dicambivoransNdbn-20, demonstrated that the cytochrome P450 monooxygenase system DsmABC was responsible for the 5-hydroxylation of 3,6-dichlorosalicylate, and proposed a dicamba catabolic pathway. This study provides a basis to elucidate the catabolism of dicamba and has benefits for the ecotoxicological study of dicamba. Furthermore, the hydroxylation of salicylate has been previously reported to be catalyzed by single-component flavoprotein or three-component Rieske non-heme iron oxygenase, whereas DsmABC was the only cytochrome P450 monooxygenase system hydroxylating salicylate and its methyl- or chloro-substituted derivatives.

scholarly journals Gut SymbiontsLactobacillus reuteriR2lc and 2010 Encode a Polyketide Synthase Cluster That Activates the Mammalian Aryl Hydrocarbon Receptor

2018 ◽  
Vol 85 (10) ◽  
Author(s):  
Mustafa Özçam ◽  
Restituto Tocmo ◽  
Jee-Hwan Oh ◽  
Amin Afrazi ◽  
Joshua D. Mezrich ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Immune System ◽  
Aryl Hydrocarbon Receptor ◽  
Gene Cluster ◽  
Polyketide Synthase ◽  
Lactobacillus Reuteri ◽  
Intestinal Inflammation ◽  
Host Immune System ◽  
Content Type ◽  
Aryl Hydrocarbon

ABSTRACTA mechanistic understanding of microbe-host interactions is critical to developing therapeutic strategies for targeted modulation of the host immune system. Different members of the gut symbiont speciesLactobacillus reuterimodulate host health by, for example, reduction of intestinal inflammation. Previously, it was shown thatL. reuteriactivates the aryl hydrocarbon receptor (AhR), a ligand-activated transcription factor that plays an important role in the mucosal immune system, by the production of tryptophan catabolites. Here, we identified a novel pathway by whichL. reuteriactivates AhR, which is independent of tryptophan metabolism. We screened a library of 36 L. reuteristrains and determined that R2lc and 2010, strains with a pigmented phenotype, are potent AhR activators. By whole-genome sequencing and comparative genomics, we identified genes unique to R2lc and 2010. Our analyses demonstrated that R2lc harbors two genetically distinct polyketide synthase (PKS) clusters, functionally unknown (fun) andpks, each carried by a multicopy plasmid. Inactivation ofpks, but notfun, abolished the ability of R2lc to activate AhR.L. reuteri2010 has a gene cluster homologous to thepkscluster in R2lc with an identical gene organization, which is also responsible for AhR activation. In conclusion, we identified a novel PKS pathway inL. reuteriR2lc and 2010 that is responsible for AhR activation.IMPORTANCETemporary changes in the composition of the microbiota, for example, by oral administration of probiotics, can modulate the host immune system. However, the underlying mechanisms by which probiotics interact with the host are often unknown. Here, we show thatLactobacillus reuteriR2lc and 2010 harbor an orthologous PKS gene cluster that activates the aryl hydrocarbon receptor (AhR). AhR is a ligand-activated transcription factor that plays a key role in a variety of diseases, including amelioration of intestinal inflammation. Understanding the mechanism by which a bacterium modulates the immune system is critical for applying rational selection strategies for probiotic supplementation. Finally, heterologous and/or optimized expression of PKS is a logical next step toward the development of next-generation probiotics to prevent and treat disease.

scholarly journals Production of Proteasome Inhibitor Syringolin A by the Endophyte Rhizobium sp. Strain AP16

2014 ◽  
Vol 80 (12) ◽  
pp. 3741-3748 ◽  
Author(s):  
Alexey Dudnik ◽  
Laurent Bigler ◽  
Robert Dudler
Keyword(s):  
Gene Cluster ◽  
Pseudomonas Syringae ◽  
Polyketide Synthase ◽  
Amino Acid Level ◽  
Proteasome Inhibitors ◽  
Proteasome Inhibition ◽  
Content Type ◽  
Animal Pathogens ◽  
Peptide Synthetase ◽  
Biocontrol Strain

ABSTRACTSyringolin A, the product of a mixed nonribosomal peptide synthetase/polyketide synthase encoded by thesylgene cluster, is a virulence factor secreted by certainPseudomonas syringaestrains. Together with the glidobactins produced by a number of beta- and gammaproteobacterial human and animal pathogens, it belongs to the syrbactins, a structurally novel class of proteasome inhibitors. In plants, proteasome inhibition by syringolin A-producingP. syringaestrains leads to the suppression of host defense pathways requiring proteasome activity, such as the ones mediated by salicylic acid and jasmonic acid. Here we report the discovery of asyl-like gene cluster with some unusual features in the alphaproteobacterial endophyteRhizobiumsp. strain AP16 that encodes a putative syringolin A-like synthetase whose components share 55% to 65% sequence identity (72% to 79% similarity) at the amino acid level. As revealed by average nucleotide identity (ANI) calculations, this strain likely belongs to the same species as biocontrol strainR. rhizogenesK84 (formely known asAgrobacterium radiobacterK84), which, however, carries a nonfunctional deletion remnant of thesyl-like gene cluster. Here we present a functional analysis of thesyl-like gene cluster ofRhizobiumsp. strain AP16 and demonstrate that this endophyte synthesizes syringolin A and some related minor variants, suggesting that proteasome inhibition by syrbactin production can be important not only for pathogens but also for endophytic bacteria in the interaction with their hosts.

scholarly journals Identification of a Polyketide Synthase Gene Responsible for Ascochitine Biosynthesis in Ascochyta fabae and Its Abrogation in Sister Taxa

mSphere ◽  
2019 ◽  
Vol 4 (5) ◽  
Author(s):  
Wonyong Kim ◽  
Judith Lichtenzveig ◽  
Robert A. Syme ◽  
Angela H. Williams ◽  
Tobin L. Peever ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Secondary Metabolite ◽  
Polyketide Synthase ◽  
Animal Health ◽  
Gene Clusters ◽  
Biosynthesis Gene Cluster ◽  
Content Type ◽  
Pathogenicity Factor ◽  
Biosynthesis Gene ◽  
Ascochyta Fabae

ABSTRACT The polyketide-derived secondary metabolite ascochitine is produced by species in the Didymellaceae family, including but not restricted to Ascochyta species pathogens of cool-season food legumes. Ascochitine is structurally similar to the well-known mycotoxin citrinin and exhibits broad-spectrum phytotoxicity and antimicrobial activities. Here, we identified a polyketide synthase (PKS) gene (denoted pksAC) responsible for ascochitine production in the filamentous fungus Ascochyta fabae. Deletion of the pksAC prevented production of ascochitine and its derivative ascochital in A. fabae. The putative ascochitine biosynthesis gene cluster comprises 11 genes that have undergone rearrangement and gain-and-loss events relative to the citrinin biosynthesis gene cluster in Monascus ruber. Interestingly, we also identified pksAC homologs in two recently diverged species, A. lentis and A. lentis var. lathyri, that are sister taxa closely related to ascochitine producers such as A. fabae and A. viciae-villosae. However, nonsense mutations have been independently introduced in coding sequences of the pksAC homologs of A. lentis and A. lentis var. lathyri that resulted in loss of ascochitine production. Despite its reported phytotoxicity, ascochitine was not a pathogenicity factor in A. fabae infection and colonization of faba bean (Vicia faba L.). Ascochitine was mainly produced from mature hyphae at the site of pycnidial formation, suggesting a possible protective role of the compound against other microbial competitors in nature. This report highlights the evolution of gene clusters harnessing the structural diversity of polyketides and a mechanism with the potential to alter secondary metabolite profiles via single nucleotide polymorphisms in closely related fungal species. IMPORTANCE Fungi produce a diverse array of secondary metabolites, many of which are of pharmacological importance whereas many others are noted for mycotoxins, such as aflatoxin and citrinin, that can threaten human and animal health. The polyketide-derived compound ascochitine, which is structurally similar to citrinin mycotoxin, has been considered to be important for pathogenicity of legume-associated Ascochyta species. Here, we identified the ascochitine polyketide synthase (PKS) gene in Ascochyta fabae and its neighboring genes that may be involved in ascochitine biosynthesis. Interestingly, the ascochitine PKS genes in other legume-associated Ascochyta species have been mutated, encoding truncated PKSs. This indicated that point mutations may have contributed to genetic diversity for secondary metabolite production in these fungi. We also demonstrated that ascochitine is not a pathogenicity factor in A. fabae. The antifungal activities and production of ascochitine during sporulation suggested that it may play a role in competition with other saprobic fungi in nature.

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