Journal articles: 'Polyketide synthase genes'

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Xu, Yuquan, Patricia Espinosa-Artiles, Vivien Schubert, Ya-ming Xu, Wei Zhang, Min Lin, A. A. Leslie Gunatilaka, Roderich Süssmuth, and István Molnár. "Characterization of the Biosynthetic Genes for 10,11-Dehydrocurvularin, a Heat Shock Response-Modulating Anticancer Fungal Polyketide from Aspergillus terreus." Applied and Environmental Microbiology 79, no. 6 (January 18, 2013): 2038–47. http://dx.doi.org/10.1128/aem.03334-12.

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ABSTRACT10,11-Dehydrocurvularin is a prevalent fungal phytotoxin with heat shock response and immune-modulatory activities. It features a dihydroxyphenylacetic acid lactone polyketide framework with structural similarities to resorcylic acid lactones like radicicol or zearalenone. A genomic locus was identified from the dehydrocurvularin producer strainAspergillus terreusAH-02-30-F7 to reveal genes encoding a pair of iterative polyketide synthases (A. terreusCURS1 [AtCURS1] and AtCURS2) that are predicted to collaborate in the biosynthesis of 10,11-dehydrocurvularin. Additional genes in this locus encode putative proteins that may be involved in the export of the compound from the cell and in the transcriptional regulation of the cluster. 10,11-Dehydrocurvularin biosynthesis was reconstituted inSaccharomyces cerevisiaeby heterologous expression of the polyketide synthases. Bioinformatic analysis of the highly reducing polyketide synthase AtCURS1 and the nonreducing polyketide synthase AtCURS2 highlights crucial biosynthetic programming differences compared to similar synthases involved in resorcylic acid lactone biosynthesis. These differences lead to the synthesis of a predicted tetraketide starter unit that forms part of the 12-membered lactone ring of dehydrocurvularin, as opposed to the penta- or hexaketide starters in the 14-membered rings of resorcylic acid lactones. TetraketideN-acetylcysteamine thioester analogues of the starter unit were shown to support the biosynthesis of dehydrocurvularin and its analogues, with yeast expressing AtCURS2 alone. Differential programming of the product template domain of the nonreducing polyketide synthase AtCURS2 results in an aldol condensation with a different regiospecificity than that of resorcylic acid lactones, yielding the dihydroxyphenylacetic acid scaffold characterized by an S-type cyclization pattern atypical for fungal polyketides.

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FUJII, Isao. "Fungal Polyketide Synthase Genes." Journal of the agricultural chemical society of Japan 72, no. 1 (1998): 56–59. http://dx.doi.org/10.1271/nogeikagaku1924.72.56.

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Komaki, Hisayuki, Ryosuke Fudou, Takashi Iizuka, Daisuke Nakajima, Koei Okazaki, Daisuke Shibata, Makoto Ojika, and Shigeaki Harayama. "PCR Detection of Type I Polyketide Synthase Genes in Myxobacteria." Applied and Environmental Microbiology 74, no. 17 (July 7, 2008): 5571–74. http://dx.doi.org/10.1128/aem.00224-08.

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ABSTRACT The diversity of type I modular polyketide synthase (PKS) was explored by PCR amplification of DNA encoding ketosynthase and acyltransferase domains in myxobacteria. The sequencing of the amplicons revealed that many PKS genes were distantly related to the published sequences. Thus, myxobacteria may be excellent resources for novel and diverse polyketides.

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Rein, K. S., P. D. L. Gibbs, A. Palacios, L. Abiy, R. Dickey, R. V. Snyder, and J. V. Lopez. "Polyketide Synthase Genes from Marine Dinoflagellates." Marine Biotechnology 5, no. 1 (February 1, 2003): 1–12. http://dx.doi.org/10.1007/s10126-002-0077-y.

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OPANOWICZ, Magdalena, Juliane BLAHA, and Martin GRUBE. "Detection of paralogous polyketide synthase genes in Parmeliaceae by specific primers." Lichenologist 38, no. 1 (December 19, 2005): 47–54. http://dx.doi.org/10.1017/s0024282905005529.

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A first assessment of paralogy in non-reducing polyketide synthases of Parmeliaceae is presented. Primers which are specific to the keto-acyl synthase domain were used to amplify gene fragments of putative non-reducing polyketide synthases from various representatives of the family. The corresponding sequences were analysed together with a selection of known polyketide synthase genes from other fungi, including lichenized fungi. The results suggest that genes from Parmeliaceae represent at least 6 paralogs. Their different positions in the tree partly correlate with the variable presence of spliceosomal introns at particular positions in the gene fragments. Because only one paralog could be unambiguously detected in each species by direct sequencing of PCR products with this approach, we tested the applicability of clade-specific primers, designed by using orthologous signature sequences. With these primers more paralogs could be detected from the same DNA extract in a number of species, but certain paralogs were consistently not amplified in these species. The paralog-specific primer approach can potentially be used for a rapid screening of PKS genes from a broader range of lichen fungi.

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Gaffoor, Iffa, and Frances Trail. "Characterization of Two Polyketide Synthase Genes Involved in Zearalenone Biosynthesis in Gibberella zeae." Applied and Environmental Microbiology 72, no. 3 (March 2006): 1793–99. http://dx.doi.org/10.1128/aem.72.3.1793-1799.2006.

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ABSTRACT Zearalenone, a mycotoxin produced by several Fusarium spp., is most commonly found as a contaminant in stored grain and has chronic estrogenic effects on mammals. Zearalenone is a polyketide derived from the sequential condensation of multiple acetate units by a polyketide synthase (PKS), but the genetics of its biosynthesis are not understood. We cloned two genes, designated ZEA1 and ZEA2, which encode polyketide synthases that participate in the biosynthesis of zearalenone by Gibberella zeae (anamorph Fusarium graminearum). Disruption of either gene resulted in the loss of zearalenone production under inducing conditions. ZEA1 and ZEA2 are transcribed divergently from a common promoter region. Quantitative PCR analysis of both PKS genes and six flanking genes supports the view that the two polyketide synthases make up the core biosynthetic unit for zearalenone biosynthesis. An appreciation of the genetics of zearalenone biosynthesis is needed to understand how zearalenone is synthesized under field conditions that result in the contamination of grain.

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Zhang, Wenjun, Brian D. Ames, Shiou-Chuan Tsai, and Yi Tang. "Engineered Biosynthesis of a Novel Amidated Polyketide, Using the Malonamyl-Specific Initiation Module from the Oxytetracycline Polyketide Synthase." Applied and Environmental Microbiology 72, no. 4 (April 2006): 2573–80. http://dx.doi.org/10.1128/aem.72.4.2573-2580.2006.

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ABSTRACT Tetracyclines are aromatic polyketides biosynthesized by bacterial type II polyketide synthases (PKSs). Understanding the biochemistry of tetracycline PKSs is an important step toward the rational and combinatorial manipulation of tetracycline biosynthesis. To this end, we have sequenced the gene cluster of oxytetracycline (oxy and otc genes) PKS genes from Streptomyces rimosus. Sequence analysis revealed a total of 21 genes between the otrA and otrB resistance genes. We hypothesized that an amidotransferase, OxyD, synthesizes the malonamate starter unit that is a universal building block for tetracycline compounds. In vivo reconstitution using strain CH999 revealed that the minimal PKS and OxyD are necessary and sufficient for the biosynthesis of amidated polyketides. A novel alkaloid (WJ35, or compound 2) was synthesized as the major product when the oxy-encoded minimal PKS, the C-9 ketoreductase (OxyJ), and OxyD were coexpressed in CH999. WJ35 is an isoquinolone compound derived from an amidated decaketide backbone and cyclized with novel regioselectivity. The expression of OxyD with a heterologous minimal PKS did not afford similarly amidated polyketides, suggesting that the oxy-encoded minimal PKS possesses novel starter unit specificity.

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Bao, Wuli, Paul J. Sheldon, Evelyn Wendt-Pienkowski, and C. Richard Hutchinson. "The Streptomyces peucetius dpsC Gene Determines the Choice of Starter Unit in Biosynthesis of the Daunorubicin Polyketide." Journal of Bacteriology 181, no. 15 (August 1, 1999): 4690–95. http://dx.doi.org/10.1128/jb.181.15.4690-4695.1999.

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ABSTRACT The starter unit used in the biosynthesis of daunorubicin is propionyl coenzyme A (CoA) rather than acetyl-CoA, which is used in the production of most of the bacterial aromatic polyketides studied to date. In the daunorubicin biosynthesis gene cluster ofStreptomyces peucetius, directly downstream of the genes encoding the β-ketoacyl:acyl carrier protein synthase subunits, are two genes, dpsC and dpsD, encoding proteins that are believed to function as the starter unit-specifying enzymes. Recombinant strains containing plasmids carrying dpsC anddpsD, in addition to other daunorubicin polyketide synthase (PKS) genes, incorporate the correct starter unit into polyketides made by these genes, suggesting that, contrary to earlier reports, the enzymes encoded by dpsC and dpsD play a crucial role in starter unit specification. Additionally, the results of a cell-free synthesis of 21-carbon polyketides from propionyl-CoA and malonyl-CoA that used the protein extracts of recombinant strains carrying other daunorubicin PKS genes to which purified DpsC was added suggest that this enzyme has the primary role in starter unit discrimination for daunorubicin biosynthesis.

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Hong, Hui, Yuhui Sun, Yongjun Zhou, Emily Stephens, Markiyan Samborskyy, and Peter F. Leadlay. "Evidence for an iterative module in chain elongation on the azalomycin polyketide synthase." Beilstein Journal of Organic Chemistry 12 (October 11, 2016): 2164–72. http://dx.doi.org/10.3762/bjoc.12.206.

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The assembly-line synthases that produce bacterial polyketide natural products follow a modular paradigm in which each round of chain extension is catalysed by a different set or module of enzymes. Examples of deviation from this paradigm, in which a module catalyses either multiple extensions or none are of interest from both a mechanistic and an evolutionary viewpoint. We present evidence that in the biosynthesis of the 36-membered macrocyclic aminopolyol lactones (marginolactones) azalomycin and kanchanamycin, isolated respectively from Streptomyces malaysiensis DSM4137 and Streptomyces olivaceus Tü4018, the first extension module catalyses both the first and second cycles of polyketide chain extension. To confirm the integrity of the azl gene cluster, it was cloned intact on a bacterial artificial chromosome and transplanted into the heterologous host strain Streptomyces lividans, which does not possess the genes for marginolactone production. When furnished with 4-guanidinobutyramide, a specific precursor of the azalomycin starter unit, the recombinant S. lividans produced azalomycin, showing that the polyketide synthase genes in the sequenced cluster are sufficient to accomplish formation of the full-length polyketide chain. This provides strong support for module iteration in the azalomycin and kanchanamycin biosynthetic pathways. In contrast, re-sequencing of the gene cluster for biosynthesis of the polyketide β-lactone ebelactone in Streptomyces aburaviensis has shown that, contrary to a recently-published proposal, the ebelactone polyketide synthase faithfully follows the colinear modular paradigm.

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KHATUN, SAYRA, ALASTAIR C. W. WAUGH, MARIA B. REDPATH, and PAUL F. LONG. "Distribution of Polyketide Synthase Genes in Bacterial Populations." Journal of Antibiotics 55, no. 1 (2002): 107–8. http://dx.doi.org/10.7164/antibiotics.55.107.

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O'Callaghan, J., and A. D. W. Dobson. "Phylogenetic analysis of polyketide synthase genes fromAspergillus ochraceus." Mycotoxin Research 22, no. 2 (June 2006): 125–33. http://dx.doi.org/10.1007/bf02956776.

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12

Ferracin, Lara Munique, Carla Beatriz Fier, Maria Lucia Carneiro Vieira, Claudia Barros Monteiro-Vitorello, Alessandro de Mello Varani, Maria Magdalena Rossi, Marcelo Müller-Santos, Marta Hiromi Taniwaki, Beatriz Thie Iamanaka, and Maria Helena Pelegrinelli Fungaro. "Strain-specific polyketide synthase genes of Aspergillus niger." International Journal of Food Microbiology 155, no. 3 (April 2012): 137–45. http://dx.doi.org/10.1016/j.ijfoodmicro.2012.01.020.

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13

Amnuaykanjanasin, Alongkorn, Suranat Phonghanpot, Nattapong Sengpanich, Supapon Cheevadhanarak, and Morakot Tanticharoen. "Insect-Specific Polyketide Synthases (PKSs), Potential PKS-Nonribosomal Peptide Synthetase Hybrids, and Novel PKS Clades in Tropical Fungi." Applied and Environmental Microbiology 75, no. 11 (April 3, 2009): 3721–32. http://dx.doi.org/10.1128/aem.02744-08.

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ABSTRACT Polyketides draw much attention because of their potential use in pharmaceutical and biotechnological applications. This study identifies an abundant pool of polyketide synthase (PKS) genes from local isolates of tropical fungi found in Thailand in three different ecological niches: insect pathogens, marine inhabitants, and lichen mutualists. We detected 149 PKS genes from 48 fungi using PCR with PKS-specific degenerate primers. We identified and classified 283 additional PKS genes from 13 fungal genomes. Phylogenetic analysis of all these PKS sequences the comprising ketosynthase (KS) conserved region and the KS-acyltransferase interdomain region yielded results very similar to those for phylogenies of the KS domain and suggested a number of remarkable points. (i) Twelve PKS genes amplified from 12 different insect-pathogenic fungi form a tight cluster, although along with two PKS genes extracted from genomes of Aspergillus niger and Aspergillus terreus, in reducing clade III. Some of these insect-specific fungal PKSs are nearly identical. (ii) We identified 38 new PKS-nonribosomal peptide synthetase hybrid genes in reducing clade II. (iii) Four distinct clades were discovered with more than 75% bootstrap support. We propose to designate the novel clade D1 with 100% bootstrap support “reducing clade V.” The newly cloned PKS genes from these tropical fungi should provide useful and diverse genetic resources for future research on the characterization of polyketide compounds synthesized by these enzymes.

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Wawrik, Boris, Lee Kerkhof, Gerben J. Zylstra, and Jerome J. Kukor. "Identification of Unique Type II Polyketide Synthase Genes in Soil." Applied and Environmental Microbiology 71, no. 5 (May 2005): 2232–38. http://dx.doi.org/10.1128/aem.71.5.2232-2238.2005.

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ABSTRACT Many bacteria, particularly actinomycetes, are known to produce secondary metabolites synthesized by polyketide synthases (PKS). Bacterial polyketides are a particularly rich source of bioactive molecules, many of which are of potential pharmaceutical relevance. To directly access PKS gene diversity from soil, we developed degenerate PCR primers for actinomycete type II KSα (ketosynthase) genes. Twenty-one soil samples were collected from diverse sources in New Jersey, and their bacterial communities were compared by terminal restriction fragment length polymorphism (TRFLP) analysis of PCR products generated using bacterial 16S rRNA gene primers (27F and 1525R) as well as an actinomycete-specific forward primer. The distribution of actinomycetes was highly variable but correlated with the overall bacterial species composition as determined by TRFLP. Two samples were identified to contain a particularly rich and unique actinomycete community based on their TRFLP patterns. The same samples also contained the greatest diversity of KSα genes as determined by TRFLP analysis of KSα PCR products. KSα PCR products from these and three additional samples with interesting TRFLP pattern were cloned, and seven novel clades of KSα genes were identified. Greatest sequence diversity was observed in a sample containing a moderate number of peaks in its KSα TRFLP. The nucleotide sequences were between 74 and 81% identical to known sequences in GenBank. One cluster of sequences was most similar to the KSα involved in ardacin (glycopeptide antibiotic) production by Kibdelosporangium aridum. The remaining sequences showed greatest similarity to the KSα genes in pathways producing the angucycline-derived antibiotics simocyclinone, pradimicin, and jasomycin.

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Lomovskaya, Natalia, Yukiko Doi-Katayama, Sylvia Filippini, Cecilia Nastro, Leonid Fonstein, Mark Gallo, Anna Luisa Colombo, and C. Richard Hutchinson. "The Streptomyces peucetius dpsY anddnrX Genes Govern Early and Late Steps of Daunorubicin and Doxorubicin Biosynthesis." Journal of Bacteriology 180, no. 9 (1998): 2379–86. http://dx.doi.org/10.1128/jb.180.9.2379-2386.1998.

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The Streptomyces peucetius dpsY and dnrXgenes govern early and late steps in the biosynthesis of the clinically valuable antitumor drugs daunorubicin (DNR) and doxorubicin (DXR). Although their deduced products resemble those of genes thought to be involved in antibiotic production in several other bacteria, this information could not be used to identify the functions ofdpsY and dnrX. Replacement of dpsYwith a mutant form disrupted by insertion of the aphIIneomycin-kanamycin resistance gene resulted in the accumulation of UWM5, the C-19 ethyl homolog of SEK43, a known shunt product of iterative polyketide synthases involved in the biosynthesis of aromatic polyketides. Hence, DpsY must act along with the other components of the DNR-DXR polyketide synthase to form 12-deoxyaklanonic acid, the earliest known intermediate of the DXR pathway. Mutation ofdnrX in the same way resulted in a threefold increase in DXR production and the disappearance of two acid-sensitive, unknown compounds from culture extracts. These results suggest thatdnrX, analogous to the role of the S. peucetius dnrH gene (C. Scotti and C. R. Hutchinson, J. Bacteriol. 178:7316–7321, 1996), may be involved in the metabolism of DNR and/or DXR to acid-sensitive compounds, possibly related to the baumycins found in many DNR-producing bacteria.

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Shen, B., R. G. Summers, E. Wendt-Pienkowski, and C. R. Hutchinson. "The Streptomyces glaucescens tcmKL polyketide synthase and tcmN polyketide cyclase genes govern the size and shape of aromatic polyketides." Journal of the American Chemical Society 117, no. 26 (July 1995): 6811–21. http://dx.doi.org/10.1021/ja00131a002.

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Gaffoor, Iffa, Daren W. Brown, Ron Plattner, Robert H. Proctor, Weihong Qi, and Frances Trail. "Functional Analysis of the Polyketide Synthase Genes in the Filamentous Fungus Gibberella zeae (Anamorph Fusarium graminearum)." Eukaryotic Cell 4, no. 11 (November 2005): 1926–33. http://dx.doi.org/10.1128/ec.4.11.1926-1933.2005.

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ABSTRACT Polyketides are a class of secondary metabolites that exhibit a vast diversity of form and function. In fungi, these compounds are produced by large, multidomain enzymes classified as type I polyketide synthases (PKSs). In this study we identified and functionally disrupted 15 PKS genes from the genome of the filamentous fungus Gibberella zeae. Five of these genes are responsible for producing the mycotoxins zearalenone, aurofusarin, and fusarin C and the black perithecial pigment. A comprehensive expression analysis of the 15 genes revealed diverse expression patterns during grain colonization, plant colonization, sexual development, and mycelial growth. Expression of one of the PKS genes was not detected under any of 18 conditions tested. This is the first study to genetically characterize a complete set of PKS genes from a single organism.

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Bacha, N., F. Mathieu, T. Liboz, and A. Lebrihi. "Polyketide synthase gene aolc35-12 controls the differential expression of ochratoxin A gene aoks1 in Aspergillus westerdijkiae." World Mycotoxin Journal 5, no. 2 (May 1, 2012): 177–86. http://dx.doi.org/10.3920/wmj2011.1374.

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Ochratoxine A (OTA), a potential human carcinogen is produced by several species of Aspergillus and Penicillium, including Aspergillus westerdijkiae. In this study a putative polyketide synthase gene aolc35-12 has been partially cloned from A. westerdijkiae. The predicted amino acid sequence of the 3.22 kb clone was found to have a high degree of similarity to other previously identified polyketide synthase genes from various OTA-producing fungi including Aspergillus ochraceus, Aspergillus niger, Aspergillus carbonarius and Penicillium nordicum. The aolc35-12 gene was disrupted and inactivated by insertion of Escherichia coli hygromycin B phosphotransferase gene, which resulted in an OTA negative mutant aoΔlc35-12. Genetic complementation confirmed aolc35-12 as OTA-polyketide synthase gene. Furthermore, study of the differential expression of aolc35-12 and a previously identified OTA-polyketide synthase gene, i.e. aoks1, in the wild-type A. westerdijkiae and aoΔlc35-12 mutant revealed that aolc35-12 could code for a certain polyketide compound complementary for the expression of aoks1 and hence for the activation of OTA biosynthesis system in A. westerdijkiae.

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Fujii, Isao, Akira Watanabe, Yuichiro Mori, and Yutaka Ebizuka. "Structures and Functional Analyses of Fungal Polyketide Synthase Genes." Actinomycetologica 12, no. 1 (1998): 1–14. http://dx.doi.org/10.3209/saj.12_1.

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Baker, Scott E., Giancarlo Perrone, Nathan M. Richardson, Antonia Gallo, and Christian P. Kubicek. "Phylogenomic analysis of polyketide synthase-encoding genes in Trichoderma." Microbiology 158, no. 1 (January 1, 2012): 147–54. http://dx.doi.org/10.1099/mic.0.053462-0.

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Behnken, Swantje, and Christian Hertweck. "Cryptic Polyketide Synthase Genes in Non-Pathogenic Clostridium SPP." PLoS ONE 7, no. 1 (January 3, 2012): e29609. http://dx.doi.org/10.1371/journal.pone.0029609.

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Lee, T., S. H. Yun, K. T. Hodge, R. A. Humber, S. B. Krasnoff, G. B. Turgeon, O. C. Yoder, and D. M. Gibson. "Polyketide synthase genes in insect- and nematode-associated fungi." Applied Microbiology and Biotechnology 56, no. 1-2 (July 1, 2001): 181–87. http://dx.doi.org/10.1007/s002530100637.

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Timsina, Brinda A., E. Stocker-Wörgötter, and Michele D. Piercey-Normore. "Monophyly of some North American species ofRamalinaand inferred polyketide synthase gene function." Botany 90, no. 12 (December 2012): 1295–307. http://dx.doi.org/10.1139/b2012-097.

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Ramalina thrausta (Ach.) Nyl., Ramalina roesleri (Hochst. Ex Schaerer) Hue, and Ramalina dilacerata (Hoffm.) Hoffm. are three common North American species that have not been placed in a phylogeny and are sympatric in their distribution leading to uncertainty about monophyly. Species characters include secondary metabolites (polyketides) in Ramalina that may be both hereditary and influenced by environmental conditions, but little is known about the function of polyketide synthase (PKS) genes. The main goal of this study was to examine the monophyly among some of the more common species in northern North America and secondarily to compare potential PKS gene function with the phylogeny. Nucleotide sequences of two genes, the internal transcribed spacer 1 of ribosomal DNA and the mitochondrial small subunit, were used to infer a phylogeny. Gene function was inferred from three PKS genes by the ratio of nonsynonymous to synonymous substitutions (dN:dS) ratios. Although seven species of Ramalina are highly supported in monophyletic clades, two other species form clusters with low support: Ramalina americana Hale is paraphyletic, and Ramalina pollinaria (Westr.) Ach. is polyphyletic. Three PKS genes were inferred to be functional but were not present in all samples. Functional PKS genes could enable adaptation to new habitats and facilitate species diversification.

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Izumi, Y., K. Ohtani, Y. Miyamoto, A. Masunaka, T. Fukumoto, K. Gomi, Y. Tada, K. Ichimura, T. L. Peever, and K. Akimitsu. "A Polyketide Synthase Gene, ACRTS2, Is Responsible for Biosynthesis of Host-Selective ACR-Toxin in the Rough Lemon Pathotype of Alternaria alternata." Molecular Plant-Microbe Interactions® 25, no. 11 (November 2012): 1419–29. http://dx.doi.org/10.1094/mpmi-06-12-0155-r.

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The rough lemon pathotype of Alternaria alternata produces host-selective ACR-toxin and causes Alternaria leaf spot disease of rough lemon (Citrus jambhiri). The structure of ACR-toxin I (MW = 496) consists of a polyketide with an α-dihydropyrone ring in a 19-carbon polyalcohol. Genes responsible for toxin production were localized to a 1.5-Mb chromosome in the genome of the rough lemon pathotype. Sequence analysis of this chromosome revealed an 8,338-bp open reading frame, ACRTS2, that was present only in the genomes of ACR-toxin-producing isolates. ACRTS2 is predicted to encode a putative polyketide synthase of 2,513 amino acids and belongs to the fungal reducing type I polyketide synthases. Typical polyketide functional domains were identified in the predicted amino acid sequence, including β-ketoacyl synthase, acyl transferase, methyl transferase, dehydratase, β-ketoreductase, and phosphopantetheine attachment site domains. Combined use of homologous recombination-mediated gene disruption and RNA silencing allowed examination of the functional role of multiple paralogs in ACR-toxin production. ACRTS2 was found to be essential for ACR-toxin production and pathogenicity of the rough lemon pathotype of A. alternata.

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Sarwar, Samreen, Mehboob Ahmed, and Shahida Hasnain. "Phylogenomic analysis of polyketide synthase genes in actinomycetes: structural analysis of KS domains and modules of polyketide synthases." International Journal of Computational Biology and Drug Design 5, no. 2 (2012): 89. http://dx.doi.org/10.1504/ijcbdd.2012.048281.

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Menzella, Hugo G., Ralph Reid, John R. Carney, Sunil S. Chandran, Sarah J. Reisinger, Kedar G. Patel, David A. Hopwood, and Daniel V. Santi. "Combinatorial polyketide biosynthesis by de novo design and rearrangement of modular polyketide synthase genes." Nature Biotechnology 23, no. 9 (August 14, 2005): 1171–76. http://dx.doi.org/10.1038/nbt1128.

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Ramette, Alban, Yvan Moënne-Loccoz, and Geneviève Défago. "Polymorphism of the Polyketide Synthase Gene phlD in Biocontrol Fluorescent Pseudomonads Producing 2,4-Diacetylphloroglucinol and Comparison of PhlD with Plant Polyketide Synthases." Molecular Plant-Microbe Interactions® 14, no. 5 (May 2001): 639–52. http://dx.doi.org/10.1094/mpmi.2001.14.5.639.

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Many biocontrol fluorescent pseudomonads can protect plants from soilborne fungal pathogens through production of the antifungal secondary metabolite 2,4-diacetylphloroglucinol (Phl). One of the phl biosynthetic genes, phlD, encodes a polyketide synthase similar to plant chalcone synthases. Here, restriction analysis of phlD from 39 Phl+ biocontrol fluorescent pseudomonads yielded seven different banding patterns. The gene was sequenced in seven strains, representing the different restriction patterns. Cluster analysis of phlD restriction data or phlD sequences indicated that phlD polymorphism was high, and two main clusters were obtained when predicted PhlD sequences were compared. When the seven PhlD sequences were studied with those of other procaryotic polyketide synthases (gram-positive bacteria) and plant chalcone synthases, however, Phl+ pseudomonads, gram-positive bacteria, and plants clustered separately. Yet, sequence analysis of active site regions for PhlD and plant chalcone synthases revealed that PhlD can be considered a member of the chalcone synthase family, which may be interpreted as convergent evolution of key enzymes involved in secondary metabolism. For the 39 Phl+ pseudomonads, a relationship was found among phlD restriction patterns, phylogenetic groups defined by 16S rDNA restriction analysis (confirmed by 16S rDNA sequencing), and production levels of Phl in vitro.

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Nakano, Chiaki, Hiroki Ozawa, Genki Akanuma, Nobutaka Funa, and Sueharu Horinouchi. "Biosynthesis of Aliphatic Polyketides by Type III Polyketide Synthase and Methyltransferase in Bacillus subtilis." Journal of Bacteriology 191, no. 15 (May 22, 2009): 4916–23. http://dx.doi.org/10.1128/jb.00407-09.

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ABSTRACT Type III polyketide synthases (PKSs) synthesize a variety of aromatic polyketides in plants, fungi, and bacteria. The bacterial genome projects predicted that probable type III PKS genes are distributed in a wide variety of gram-positive and -negative bacteria. The gram-positive model microorganism Bacillus subtilis contained the bcsA-ypbQ operon, which appeared to encode a type III PKS and a methyltransferase, respectively. Here, we report the characterization of bcsA (renamed bpsA, for Bacillus pyrone synthase, on the basis of its function) and ypbQ, which are involved in the biosynthesis of aliphatic polyketides. In vivo analysis demonstrated that BpsA was a type III PKS catalyzing the synthesis of triketide pyrones from long-chain fatty acyl-coenzyme A (CoA) thioesters as starter substrates and malonyl-CoA as an extender substrate, and YpbQ was a methyltransferase acting on the triketide pyrones to yield alkylpyrone methyl ethers. YpbQ thus was named BpsB because of its functional relatedness to BpsA. In vitro analysis with histidine-tagged BpsA revealed that it used broad starter substrates and produced not only triketide pyrones but also tetraketide pyrones and alkylresorcinols. Although the aliphatic polyketides were expected to localize in the membrane and play some role in modulating the rigidity and properties of the membrane, no detectable phenotypic changes were observed for a B. subtilis mutant containing a whole deletion of the bpsA-bpsB operon.

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Rego, Adriana, António G. G. Sousa, João P. Santos, Francisco Pascoal, João Canário, Pedro N. Leão, and Catarina Magalhães. "Diversity of Bacterial Biosynthetic Genes in Maritime Antarctica." Microorganisms 8, no. 2 (February 18, 2020): 279. http://dx.doi.org/10.3390/microorganisms8020279.

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Bacterial natural products (NPs) are still a major source of new drug leads. Polyketides (PKs) and non-ribosomal peptides (NRP) are two pharmaceutically important families of NPs and recent studies have revealed Antarctica to harbor endemic polyketide synthase (PKS) and non-ribosomal peptide synthetase (NRPS) genes, likely to be involved in the production of novel metabolites. Despite this, the diversity of secondary metabolites genes in Antarctica is still poorly explored. In this study, a computational bioprospection approach was employed to study the diversity and identity of PKS and NRPS genes to one of the most biodiverse areas in maritime Antarctica—Maxwell Bay. Amplicon sequencing of soil samples targeting ketosynthase (KS) and adenylation (AD) domains of PKS and NRPS genes, respectively, revealed abundant and unexplored chemical diversity in this peninsula. About 20% of AD domain sequences were only distantly related to characterized biosynthetic genes. Several PKS and NRPS genes were found to be closely associated to recently described metabolites including those from uncultured and candidate phyla. The combination of new approaches in computational biology and new culture-dependent and -independent strategies is thus critical for the recovery of the potential novel chemistry encoded in Antarctica microorganisms.

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Cheng, Yi-Qiang, Min Yang, and Andrea M. Matter. "Characterization of a Gene Cluster Responsible for the Biosynthesis of Anticancer Agent FK228 in Chromobacterium violaceum No. 968." Applied and Environmental Microbiology 73, no. 11 (March 30, 2007): 3460–69. http://dx.doi.org/10.1128/aem.01751-06.

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ABSTRACT A gene cluster responsible for the biosynthesis of anticancer agent FK228 has been identified, cloned, and partially characterized in Chromobacterium violaceum no. 968. First, a genome-scanning approach was applied to identify three distinctive C. violaceum no. 968 genomic DNA clones that code for portions of nonribosomal peptide synthetase and polyketide synthase. Next, a gene replacement system developed originally for Pseudomonas aeruginosa was adapted to inactivate the genomic DNA-associated candidate natural product biosynthetic genes in vivo with high efficiency. Inactivation of a nonribosomal peptide synthetase-encoding gene completely abolished FK228 production in mutant strains. Subsequently, the entire FK228 biosynthetic gene cluster was cloned and sequenced. This gene cluster is predicted to encompass a 36.4-kb DNA region that includes 14 genes. The products of nine biosynthetic genes are proposed to constitute an unusual hybrid nonribosomal peptide synthetase-polyketide synthase-nonribosomal peptide synthetase assembly line including accessory activities for the biosynthesis of FK228. In particular, a putative flavin adenine dinucleotide-dependent pyridine nucleotide-disulfide oxidoreductase is proposed to catalyze disulfide bond formation between two sulfhydryl groups of cysteine residues as the final step in FK228 biosynthesis. Acquisition of the FK228 biosynthetic gene cluster and acclimation of an efficient genetic system should enable genetic engineering of the FK228 biosynthetic pathway in C. violaceum no. 968 for the generation of structural analogs as anticancer drug candidates.

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Lopanik, Nicole B., Nancy M. Targett, and Niels Lindquist. "Isolation of Two Polyketide Synthase Gene Fragments from the Uncultured Microbial Symbiont of the Marine Bryozoan Bugula neritina." Applied and Environmental Microbiology 72, no. 12 (September 22, 2006): 7941–44. http://dx.doi.org/10.1128/aem.01277-06.

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ABSTRACT “Candidatus Endobugula sertula,” the uncultured microbial symbiont of the bryozoan Bugula neritina, produces ecologically and biomedically important polyketide metabolites called bryostatins. We isolated two gene fragments from B. neritina larvae that have high levels of similarity to polyketide synthase genes. These gene fragments are clearly associated with the symbiont and not with the host.

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Williams, Ernest P., Tsvetan R. Bachvaroff, and Allen R. Place. "A Global Approach to Estimating the Abundance and Duplication of Polyketide Synthase Domains in Dinoflagellates." Evolutionary Bioinformatics 17 (January 2021): 117693432110318. http://dx.doi.org/10.1177/11769343211031871.

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Many dinoflagellate species make toxins in a myriad of different molecular configurations but the underlying chemistry in all cases is presumably via modular synthases, primarily polyketide synthases. In many organisms modular synthases occur as discrete synthetic genes or domains within a gene that act in coordination thus forming a module that produces a particular fragment of a natural product. The modules usually occur in tandem as gene clusters with a syntenic arrangement that is often predictive of the resultant structure. Dinoflagellate genomes however are notoriously complex with individual genes present in many tandem repeats and very few synthetic modules occurring as gene clusters, unlike what has been seen in bacteria and fungi. However, modular synthesis in all organisms requires a free thiol group that acts as a carrier for sequential synthesis called a thiolation domain. We scanned 47 dinoflagellate transcriptomes for 23 modular synthase domain models and compared their abundance among 10 orders of dinoflagellates as well as their co-occurrence with thiolation domains. The total count of domain types was quite large with over thirty-thousand identified, 29 000 of which were in the core dinoflagellates. Although there were no specific trends in domain abundance associated with types of toxins, there were readily observable lineage specific differences. The Gymnodiniales, makers of long polyketide toxins such as brevetoxin and karlotoxin had a high relative abundance of thiolation domains as well as multiple thiolation domains within a single transcript. Orders such as the Gonyaulacales, makers of small polyketides such as spirolides, had fewer thiolation domains but a relative increase in the number of acyl transferases. Unique to the core dinoflagellates, however, were thiolation domains occurring alongside tetratricopeptide repeats that facilitate protein-protein interactions, especially hexa and hepta-repeats, that may explain the scaffolding required for synthetic complexes capable of making large toxins. Clustering analysis for each type of domain was also used to discern possible origins of duplication for the multitude of single domain transcripts. Single domain transcripts frequently clustered with synonymous domains from multi-domain transcripts such as the BurA and ZmaK like genes as well as the multi-ketosynthase genes, sometimes with a large degree of apparent gene duplication, while fatty acid synthesis genes formed distinct clusters. Surprisingly the acyl-transferases and ketoreductases involved in fatty acid synthesis (FabD and FabG, respectively) were found in very large clusters indicating an unprecedented degree of gene duplication for these genes. These results demonstrate a complex evolutionary history of core dinoflagellate modular synthases with domain specific duplications throughout the lineage as well as clues to how large protein complexes can be assembled to synthesize the largest natural products known.

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Schmitt, Imke, Stefanie Kautz, and H. Thorsten Lumbsch. "6-MSAS-like polyketide synthase genes occur in lichenized ascomycetes." Mycological Research 112, no. 2 (February 2008): 289–96. http://dx.doi.org/10.1016/j.mycres.2007.08.023.

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Komaki, Hisayuki, and Shigeaki Harayama. "Sequence Diversity of Type-II Polyketide Synthase Genes in Streptomyces." Actinomycetologica 20, no. 2 (2006): 42–48. http://dx.doi.org/10.3209/saj.20.42.

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Rojas, Juan Diego, Lara Durães Sette, Welington L. de Araujo, Mateus Schreiner Garcez Lopes, Luiziana Ferreira da Silva, Renata L. A. Furlan, and Gabriel Padilla. "The Diversity of Polyketide Synthase Genes from Sugarcane-Derived Fungi." Microbial Ecology 63, no. 3 (September 22, 2011): 565–77. http://dx.doi.org/10.1007/s00248-011-9938-0.

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Baker, Scott E., Scott Kroken, Patrik Inderbitzin, Thipa Asvarak, Bi-Yu Li, Liang Shi, O. C. Yoder, and B. Gillian Turgeon. "Two Polyketide Synthase-Encoding Genes Are Required for Biosynthesis of the Polyketide Virulence Factor, T-toxin, by Cochliobolus heterostrophus." Molecular Plant-Microbe Interactions® 19, no. 2 (February 2006): 139–49. http://dx.doi.org/10.1094/mpmi-19-0139.

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Cochliobolus heterostrophus race T, causal agent of southern corn leaf blight, requires T-toxin (a family of C35 to C49 polyketides) for high virulence on T-cytoplasm maize. Production of T-toxin is controlled by two unlinked loci, Tox1A and Tox1B, carried on 1.2 Mb of DNA not found in race O, a mildly virulent form of the fungus that does not produce T-toxin, or in any other Cochliobolus spp. or closely related fungus. PKS1, a polyketide synthase (PKS)-encoding gene at Tox1A, and DEC1, a decarboxylase-encoding gene at Tox1B, are necessary for T-toxin production. Although there is evidence that additional genes are required for Ttoxin production, efforts to clone them have been frustrated because the genes are located in highly repeated, A+T-rich DNA. To overcome this difficulty, ligation specificity-based expression analysis display (LEAD), a comparative amplified fragment length polymorphism/gel fractionation/capillary sequencing procedure, was applied to cDNAs from a near-isogenic pair of race T (Tox1+) and race O (Tox1-) strains. This led to discovery of PKS2, a second PKS-encoding gene that maps at Tox1A and is required for both Ttoxin biosynthesis and high virulence to maize. Thus, the carbon chain of each T-toxin family member likely is assembled by action of two PKSs, which produce two polyketides, one of which may act as the starter unit for biosynthesis of the mature T-toxin molecule.

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Lee, Bee-Na, Scott Kroken, David Y. T. Chou, Barbara Robbertse, O. C. Yoder, and B. Gillian Turgeon. "Functional Analysis of All Nonribosomal Peptide Synthetases in Cochliobolus heterostrophus Reveals a Factor, NPS6, Involved in Virulence and Resistance to Oxidative Stress." Eukaryotic Cell 4, no. 3 (March 2005): 545–55. http://dx.doi.org/10.1128/ec.4.3.545-555.2005.

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ABSTRACT Nonribosomal peptides, made by nonribosomal peptide synthetases, have diverse biological activities, including roles as fungal virulence effectors. Inspection of the genome of Cochliobolus heterostrophus, a fungal pathogen of maize and a member of a genus noted for secondary metabolite production, revealed eight multimodular nonribosomal peptide synthase (NPS) genes and three monomodular NPS-like genes, one of which encodes a nonribosomal peptide synthetase/polyketide synthase hybrid enzyme presumed to be involved in synthesis of a peptide/polyketide molecule. Deletion of each NPS gene and phenotypic analyses showed that the product of only one of these genes, NPS6, is required for normal virulence on maize. NPS6 is also required for resistance to hydrogen peroxide, suggesting it may protect the fungus from oxidative stress. This and all other nps mutants had normal growth, mating ability, and appressoria. Real-time PCR analysis showed that expression of all NPS genes is low (relative to that of actin), that all (except possibly NPS2) are expressed during vegetative growth, and that expression is induced by nitrogen starvation. Only NPS6 is unfailingly conserved among euascomycete fungi, including plant and human pathogens and saprobes, suggesting the possibility that NPS6 activity provides oxidative stress protection during both saprobic and parasitic growth.

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Trindade-Silva, Amaro E., Cintia P. J. Rua, Bruno G. N. Andrade, Ana Carolina Paulo Vicente, Genivaldo G. Z. Silva, Roberto G. S. Berlinck, and Fabiano L. Thompson. "Polyketide Synthase Gene Diversity within the Microbiome of the Sponge Arenosclera brasiliensis, Endemic to the Southern Atlantic Ocean." Applied and Environmental Microbiology 79, no. 5 (December 28, 2012): 1598–605. http://dx.doi.org/10.1128/aem.03354-12.

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ABSTRACTMicrobes associated with marine sponges are considered important producers of bioactive, structurally unique polyketides. The synthesis of such secondary metabolites involves type I polyketide synthases (PKSs), which are enzymes that reach a maximum complexity degree in bacteria. The Haplosclerida spongeArenosclera brasiliensishosts a complex microbiota and is the source of arenosclerins, alkaloids with cytotoxic and antibacterial activity. In the present investigation, we performed high-throughput sequencing of the ketosynthase (KS) amplicon to investigate the diversity of PKS genes present in the metagenome ofA. brasiliensis. Almost 4,000 ketosynthase reads were recovered, with about 90% annotated automatically as bacterial. A total of 235 bacterial KS contigs was rigorously assembled from this sequence pool and submitted to phylogenetic analysis. A great diversity of six type I PKS groups has been consistently detected in our phylogenetic reconstructions, including a novel andA. brasiliensis-exclusive group. Our study is the first to reveal the diversity of type I PKS genes inA. brasiliensisas well as the potential of its microbiome to serve as a source of new polyketides.

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Chooi, Yit-Heng, Mariano Jordi Muria-Gonzalez, Oliver L. Mead, and Peter S. Solomon. "SnPKS19Encodes the Polyketide Synthase for Alternariol Mycotoxin Biosynthesis in the Wheat Pathogen Parastagonospora nodorum." Applied and Environmental Microbiology 81, no. 16 (May 29, 2015): 5309–17. http://dx.doi.org/10.1128/aem.00278-15.

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ABSTRACTAlternariol (AOH) is an important mycotoxin from theAlternariafungi. AOH was detected for the first time in the wheat pathogenParastagonospora nodorumin a recent study. Here, we exploited reverse genetics to demonstrate that SNOG_15829 (SnPKS19), a close homolog ofPenicillium aethiopicumnorlichexanthone (NLX) synthase genegsfA, is required for AOH production. We further validate thatSnPKS19is solely responsible for AOH production by heterologous expression inAspergillus nidulans. The expression profile ofSnPKS19based on previousP. nodorummicroarray data correlated with the presence of AOHin vitroand its absencein planta. Subsequent characterization of the ΔSnPKS19mutants showed thatSnPKS19and AOH are not involved in virulence and oxidative stress tolerance. Identification and characterization of theP. nodorumSnPKS19cast light on a possible alternative AOH synthase gene inAlternaria alternataand allowed us to survey the distribution of AOH synthase genes in other fungal genomes. We further demonstrate that phylogenetic analysis could be used to differentiate between AOH synthases and the closely related NLX synthases. This study provides the basis for studying the genetic regulation of AOH production and for development of molecular diagnostic methods for detecting AOH-producing fungi in the future.

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Bangera, M. Gita, and Linda S. Thomashow. "Identification and Characterization of a Gene Cluster for Synthesis of the Polyketide Antibiotic 2,4-Diacetylphloroglucinol from Pseudomonas fluorescens Q2-87." Journal of Bacteriology 181, no. 10 (1999): 3155–63. http://dx.doi.org/10.1128/jb.181.10.3155-3163.1999.

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The polyketide metabolite 2,4-diacetylphloroglucinol (2,4-DAPG) is produced by many strains of fluorescent Pseudomonas spp. with biocontrol activity against soilborne fungal plant pathogens. Genes required for 2,4-DAPG synthesis by P. fluorescensQ2-87 are encoded by a 6.5-kb fragment of genomic DNA that can transfer production of 2,4-DAPG to 2,4-DAPG-nonproducing recipientPseudomonas strains. In this study the nucleotide sequence was determined for the 6.5-kb fragment and flanking regions of genomic DNA from strain Q2-87. Six open reading frames were identified, four of which (phlACBD) comprise an operon that includes a set of three genes (phlACB) conserved between eubacteria and archaebacteria and a gene (phlD) encoding a polyketide synthase with homology to chalcone and stilbene synthases from plants. The biosynthetic operon is flanked on either side by phlEand phlF, which code respectively for putative efflux and regulatory (repressor) proteins. Expression in Escherichia coli of phlA, phlC, phlB, andphlD, individually or in combination, identified a novel polyketide biosynthetic pathway in which PhlD is responsible for the production of monoacetylphloroglucinol (MAPG). PhlA, PhlC, and PhlB are necessary to convert MAPG to 2,4-DAPG, and they also may function in the synthesis of MAPG.

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Song, Chaoyi, Ji Luan, Ruijuan Li, Chanjuan Jiang, Yu Hou, Qingwen Cui, Tianqi Cui, et al. "RedEx: a method for seamless DNA insertion and deletion in large multimodular polyketide synthase gene clusters." Nucleic Acids Research 48, no. 22 (October 29, 2020): e130-e130. http://dx.doi.org/10.1093/nar/gkaa956.

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Abstract Biosynthesis reprograming is an important way to diversify chemical structures. The large repetitive DNA sequences existing in polyketide synthase genes make seamless DNA manipulation of the polyketide biosynthetic gene clusters extremely challenging. In this study, to replace the ethyl group attached to the C-21 of the macrolide insecticide spinosad with a butenyl group by refactoring the 79-kb gene cluster, we developed a RedEx method by combining Redαβ mediated linear-circular homologous recombination, ccdB counterselection and exonuclease mediated in vitro annealing to insert an exogenous extension module in the polyketide synthase gene without any extra sequence. RedEx was also applied for seamless deletion of the rhamnose 3′-O-methyltransferase gene in the spinosad gene cluster to produce rhamnosyl-3′-desmethyl derivatives. The advantages of RedEx in seamless mutagenesis will facilitate rational design of complex DNA sequences for diverse purposes.

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Fu, Fang-Fang, Zhaodong Hao, Pengkai Wang, Ye Lu, Liang-Jiao Xue, Guoyu Wei, Yanli Tian, et al. "Genome Sequence and Comparative Analysis of Colletotrichum gloeosporioides Isolated from Liriodendron Leaves." Phytopathology® 110, no. 7 (July 2020): 1260–69. http://dx.doi.org/10.1094/phyto-12-19-0452-r.

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Colletotrichum gloeosporioides is a hemibiotrophic pathogen causing significant losses to economically important crops and forest trees, including Liriodendron. To explore the interaction between C. gloeosporioides and Liriodendron and to identify the candidate genes determining the pathogenesis, we sequenced and assembled the whole genome of C. gloeosporioides Lc1 (CgLc1) using PacBio and Illumina next generation sequencing and performed a comparative genomic analysis between CgLc1 and Cg01, the latter being a described endophytic species of the C. gloeosporioides complex. Gene structure prediction identified 15,744 protein-coding genes and 837 noncoding RNAs. Species-specific genes were characterized using an ortholog analysis followed by a pathway enrichment analysis, which showed that genes specific to CgLc1 were enriched for the arginine biosynthetic process. Furthermore, genome synteny analysis revealed that most of the protein-coding genes fell into collinear blocks. However, two clusters of polyketide synthase genes were identified to be specific for CgLc1, suggesting that they might have an important role in virulence control. Transcriptional regulators coexpressed with polyketide synthase genes were detected through a Weighted Correlation Network Analysis. Taken together, this work provides new insight into the virulence- and pathogenesis-associated genes present in C. gloeosporioides and its possible lifestyle.

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Kumar, Amrita, and Brian E. Ellis. "A family of polyketide synthase genes expressed in ripening Rubus fruits." Phytochemistry 62, no. 3 (February 2003): 513–26. http://dx.doi.org/10.1016/s0031-9422(02)00572-1.

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Kubota, Takaaki, Yoshiro Iinuma, and Jun'ichi Kobayashi. "Cloning of Polyketide Synthase Genes from Amphidinolide-Producing Dinoflagellate Amphidinium sp." Biological & Pharmaceutical Bulletin 29, no. 7 (2006): 1314–18. http://dx.doi.org/10.1248/bpb.29.1314.

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Zucko, J., N. Skunca, T. Curk, B. Zupan, P. F. Long, J. Cullum, R. H. Kessin, and D. Hranueli. "Polyketide synthase genes and the natural products potential of Dictyostelium discoideum." Bioinformatics 23, no. 19 (July 27, 2007): 2543–49. http://dx.doi.org/10.1093/bioinformatics/btm381.

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Bingle, Lewis E. H., Thomas J. Simpson, and Colin M. Lazarus. "Ketosynthase Domain Probes Identify Two Subclasses of Fungal Polyketide Synthase Genes." Fungal Genetics and Biology 26, no. 3 (April 1999): 209–23. http://dx.doi.org/10.1006/fgbi.1999.1115.

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Hansen, Frederik T., Jens L. Sørensen, Henriette Giese, Teis E. Sondergaard, and Rasmus J. N. Frandsen. "Quick guide to polyketide synthase and nonribosomal synthetase genes in Fusarium." International Journal of Food Microbiology 155, no. 3 (April 2012): 128–36. http://dx.doi.org/10.1016/j.ijfoodmicro.2012.01.018.

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Studt, Lena, Philipp Wiemann, Karin Kleigrewe, Hans-Ulrich Humpf, and Bettina Tudzynski. "Biosynthesis of Fusarubins Accounts for Pigmentation of Fusarium fujikuroi Perithecia." Applied and Environmental Microbiology 78, no. 12 (April 6, 2012): 4468–80. http://dx.doi.org/10.1128/aem.00823-12.

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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.

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Woo, Patrick C. Y., Susanna K. P. Lau, Bin Liu, James J. Cai, Ken T. K. Chong, Herman Tse, Richard Y. T. Kao, Che-Man Chan, Wang-Ngai Chow, and Kwok-Yung Yuen. "Draft Genome Sequence of Penicillium marneffei Strain PM1." Eukaryotic Cell 10, no. 12 (November 30, 2011): 1740–41. http://dx.doi.org/10.1128/ec.05255-11.

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ABSTRACT Penicillium marneffei is the most important thermal dimorphic, pathogenic fungus endemic in China and Southeast Asia and is particularly important in HIV-positive patients. We report the 28,887,485-bp draft genome sequence of P. marneffei , which contains its complete mitochondrial genome, sexual cycle genes, a high diversity of Mp1p homologues, and polyketide synthase genes.

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Fieseler, Lars, Ute Hentschel, Lubomir Grozdanov, Andreas Schirmer, Gaiping Wen, Matthias Platzer, Siniša Hrvatin, Daniel Butzke, Katrin Zimmermann, and Jörn Piel. "Widespread Occurrence and Genomic Context of Unusually Small Polyketide Synthase Genes in Microbial Consortia Associated with Marine Sponges." Applied and Environmental Microbiology 73, no. 7 (February 9, 2007): 2144–55. http://dx.doi.org/10.1128/aem.02260-06.

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ABSTRACT Numerous marine sponges harbor enormous amounts of as-yet-uncultivated bacteria in their tissues. There is increasing evidence that these symbionts play an important role in the synthesis of protective metabolites, many of which are of great pharmacological interest. In this study, genes for the biosynthesis of polyketides, one of the most important classes of bioactive natural products, were systematically investigated in 20 demosponge species from different oceans. Unexpectedly, the sponge metagenomes were dominated by a ubiquitously present, evolutionarily distinct, and highly sponge-specific group of polyketide synthases (PKSs). Open reading frames resembling animal fatty acid genes were found on three corresponding DNA regions isolated from the metagenomes of Theonella swinhoei and Aplysina aerophoba. Their architecture suggests that methyl-branched fatty acids are the metabolic product. According to a phylogenetic analysis of housekeeping genes, at least one of the PKSs belongs to a bacterium of the Deinococcus-Thermus phylum. The results provide new insights into the chemistry of sponge symbionts and allow inference of a detailed phylogeny of the diverse functional PKS types present in sponge metagenomes. Based on these qualitative and quantitative data, we propose a significantly simplified strategy for the targeted isolation of biomedically relevant PKS genes from complex sponge-symbiont associations.

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Journal articles on the topic 'Polyketide synthase genes'

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