Diversity of polyketide synthase gene sequences in Aspergillus species

Varga, János; Rigó, Krisztina; Kocsubé, Sándor; Farkas, Balázs; Pál, Károly

doi:10.1016/s0923-2508(03)00169-4

Cited by 44 publications

(44 citation statements)

References 57 publications

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“…Fungal polyketide synthases (PKSs) are responsible for the biosynthesis of several mycotoxins and other secondary metabolites through sequential decarboxylative condensations of short carboxylic acid units similarly to fatty acid synthases [1,2]. Recently, several genomes of filamentous fungi have been sequenced.…”

Section: Introductionmentioning

confidence: 99%

“…Fungal PKSs are classified into three groups based on the molecular architecture of the genes: (i) PKSs for nonreduced polyketides, (ii) PKSs for partially reduced polyketides, and (iii) PKSs for reduced polyketides [1,7]. They are defined as iterative type I PKSs because they usually contain only a single set of domains, in contrast to the noniterative modular type I PKSs and monofunctional type II PKSs found in bacteria [7 -9].…”

Section: Introductionmentioning

confidence: 99%

“…Many PKSs, especially those for reduced polyketides, also contain additional domains, such as b-ketoacyl reductase, dehydratase, enoylreductase, and methyltransferase [7]. A single-modular PKS can catalyze multiple cycles of chain elongation [1,8,10].…”

Section: Introductionmentioning

confidence: 99%

“…A. ochraceus is able to contaminate many food commodities including cereals, coffee, grapes, and others, often producing several mycotoxins such as ochratoxin A (OTA), viomellein, and penicillic acid [1]. A. carbonarius is considered to be responsible for OTA contamination in grapes, wines, and coffee [11].…”

Section: Introductionmentioning

confidence: 99%

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Amplification and diversity analysis of ketosynthase domains of putative polyketide synthase genes in Aspergillus ochraceus and Aspergillus carbonarius producers of ochratoxin A

Atoui

Dao

Mathieu

et al. 2006

Molecular Nutrition Food Res

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The diversity of polyketide synthase (PKS) genes in Aspergillus ochraceus NRRL 3174 and Aspergillus carbonarius 2Mu134 has been investigated using different primer pairs previously developed for the ketosynthase (KS) domain of fungal PKSs. Nine different KS domain sequences in A. ochraceus NRRL 3174 as well as five different KS domain sequences in A. carbonarius 2Mu134 have been identified. The identified KS fragments were distributed in five different clusters on the phylogenetic tree, indicating that they most probably represent PKSs responsible for different functions.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Amplification and diversity analysis of ketosynthase domains of putative polyketide synthase genes in Aspergillus ochraceus and Aspergillus carbonarius producers of ochratoxin A

Atoui

Dao

Mathieu

et al. 2006

Molecular Nutrition Food Res

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“…On the basis of the data from this large scale sequence of P. coprobium, the tblastn search (protein-DNA) (Basic Local Alignment Search Tool, NCBI BLAST) was carried out comparing with five proteins known to be involved in polyketide and terpenoid biosynthesis. 13,14 These five proteins were three polyketide synthases (RAM2-like protein of P. marneffei (GenBank accession no. Q0MR08)), the polyketide synthetase (PKS) PksP of A. fumigatus A1163 (GenBank accession no.…”

Section: Resultsmentioning

confidence: 99%

Characterization of two cytochrome P450 monooxygenase genes of the pyripyropene biosynthetic gene cluster from Penicillium coprobium

Okawa

Yamamoto

et al. 2011

J Antibiot

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Pyripyropenes are potent inhibitors of acyl-CoA:cholesterol acyltransferase, which were initially discovered to be produced by Aspergillus fumigatus. Recently, Penicillium coprobium PF1169 has also found to produce pyripyropene A (PyA), which exhibits insecticidal properties. Pyripyropenes are natural hybrid products of both terpenoid and polyketide origin. In our research, based on data generated using the Genome Sequencer FLX for P. coprobium PF1169, we predicted the biosynthetic gene cluster of PyA by blast analysis comparing with polyketide synthase and prenyltransferase of other species. By screening the genomic fosmid library, nine open reading frames (ppb1 to ppb9) related to the biosynthesis of PyA were deduced. Among them, two cytochrome P450 monooxygenase genes (ppb3 and ppb4) were separately introduced into the model fungus A. oryzae. Bioconversion of certain predicted intermediates in the transformants has elucidated the manner of hydroxylation in the biosynthetic pathway by the expressed products of these two genes (P450-1 and P450-2). That is, P450-1 exhibits monooxygenase activity and plays the hydroxylation role at C-11 of pyripyropene E. While P450-2 plays an active role in the hydroxylation of C-7 and C-13 of pyripyropene O. Keywords: cytochrome P450 monooxygenase; Penicillium coprobium; polyketide synthase; prenyltransferase; pyripyropene INTRODUCTION Pyripyropene A (PyA) has been found to be produced by Penicillium coprobium PF1169 1 and exhibits insecticidal properties. 2 The isomers of pyripyropenes A to L, initially isolated from the fermentation broth of Aspergillus fumigatus FO-1289FO- in 1993 3), have been regarded as potent inhibitors of acyl-CoA:cholesterol acyltransferase, the enzyme responsible for intracellular esterification of cholesterol. It has been reported that PyA displays insecticidal activity against Helicoverpa zea larvae. 2 The isomers of pyripyropenes A, B and D from a marine-derived fungus Aspergillus sp. GF5 were recently found to exhibit selective anti-growth properties against human umbilical vein endothelial cells. 4 Previous biochemical experiments partially delineated the PyA biosynthetic pathway. 5 Recently, the early steps of its biosynthesis in A. fumigatus FO-1289 were precisely elucidated by applying a transgenic approach with heterologous fungus. Nevertheless, hydroxylation and acetylation mechanisms for the late steps had remained unknown.We focused on cytochrome P450s, which are candidate catalysts at this hydroxylation step. Cytochrome P450 enzymes constitute a superfamily that typically catalyze the oxidation of numerous endogenous and exogenous compounds in bacteria, fungi, plants, insects and vertebrates. [6][7][8] The cytochrome acts as a terminal oxidase accepting electrons from NADPH, through NADPH cytochrome P450 reductase, or from NADH through cytochrome b 5 . The exogenous compounds metabolized in this way include numerous pesticides and insecticides. 9 In this paper, we describe the cloning and structural analysis of a 24 kb genomic DNA regi...

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Discovery of fungal enzymes and pathways

Mitrović

Glieder

2015

Fungal Biomolecules

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Diversity of polyketide synthase gene sequences in Aspergillus species

Cited by 44 publications

References 57 publications

Amplification and diversity analysis of ketosynthase domains of putative polyketide synthase genes in Aspergillus ochraceus and Aspergillus carbonarius producers of ochratoxin A

Amplification and diversity analysis of ketosynthase domains of putative polyketide synthase genes in Aspergillus ochraceus and Aspergillus carbonarius producers of ochratoxin A

Characterization of two cytochrome P450 monooxygenase genes of the pyripyropene biosynthetic gene cluster from Penicillium coprobium

Discovery of fungal enzymes and pathways

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