Characterization of a non-reducing polyketide synthase gene from lichen Dirinaria applanata

Ramanathan, V.; Hariharan, G.; Venkataraman, Gayatri; Parida, Ajay

doi:10.1016/j.phytochem.2009.04.007

Cited by 24 publications

(12 citation statements)

References 36 publications

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“…The successful isolation and functional analysis of PKSs will be the first step in the production of lichen products via genetic approaches. Although many studies of lichen PKSs have been conducted (Chooi et al, 2008;Brunauer et al, 2009;Valarmathi et al, 2009), only one study has been performed on reducing-PKSs in lichens to date, namely SocPKS1 of Solorina crocea (Gagunashvili et al, 2009).…”

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confidence: 99%

Isolation and characterization of a reducing polyketide synthase gene from the lichen-forming fungus Usnea longissima

et al. 2011

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The reducing polyketide synthases found in filamentous fungi are involved in the biosynthesis of many drugs and toxins. Lichens produce bioactive polyketides, but the roles of reducing polyketide synthases in lichens remain to be clearly elucidated. In this study, a reducing polyketide synthase gene (U1PKS3) was isolated and characterized from a cultured mycobiont of Usnea longissima. Complete sequence information regarding U1PKS3 (6,519 bp) was obtained by screening a fosmid genomic library. A U1PKS3 sequence analysis suggested that it contains features of a reducing fungal type I polyketide synthase with β-ketoacyl synthase (KS), acyltransferase (AT), dehydratase (DH), enoyl reductase (ER), ketoacyl reducatse (KR), and acyl carrier protein (ACP) domains. This domain structure was similar to the structure of ccRadsl, which is known to be involved in resorcylic acid lactone biosynthesis in Chaetomium chiversii. The results of phylogenetic analysis located U1PKS3 in the clade of reducing polyketide synthases. RT-PCR analysis results demonstrated that UIPKS3 had six intervening introns and that UIPKS3 expression was upregulated by glucose, sorbitol, inositol, and mannitol.

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confidence: 99%

Isolation and characterization of a reducing polyketide synthase gene from the lichen-forming fungus Usnea longissima

et al. 2011

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“…Carbon and nitrogen sources influence secondary metabolism in cultured LFF [18, 34, 35], and also influence the expression of biosynthetic genes. We analyzed gene expression in different nutrient conditions.…”

Section: Discussionmentioning

confidence: 99%

“…The PKS genes of β-orcinols are similar and could belong to the NR-PKS group, with a methyltransferase (MeT) domain [14, 15]. To date, only a few lichen PKSs, mostly NR-PKSs, have been analyzed [14, 15, 16, 17, 18, 19]. …”

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Three New Non-reducing Polyketide Synthase Genes from the Lichen-Forming Fungus Usnea longissima

Wang

Cheong

et al. 2014

Mycobiology

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Usnea longissima has a long history of use as a traditional medicine. Several bioactive compounds, primarily belonging to the polyketide family, have been isolated from U. longissima. However, the genes for the biosynthesis of these compounds are yet to be identified. In the present study, three different types of non-reducing polyketide synthases (UlPKS2, UlPKS4, and UlPKS6) were identified from a cultured lichen-forming fungus of U. longissima. Phylogenetic analysis of product template domains showed that UlPKS2 and UlPKS4 belong to group IV, which includes the non-reducing polyketide synthases with an methyltransferase (MeT) domain that are involved in methylorcinol-based compound synthesis; UlPKS6 was found to belong to group I, which includes the non-reducing polyketide synthases that synthesize single aromatic ring polyketides, such as orsellinic acid. Reverse transcriptase-PCR analysis demonstrated that UlPKS2 and UlPKS4 were upregulated by sucrose; UlPKS6 was downregulated by asparagine, glycine, and alanine.

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“…Several types of fungi have been shown to have biosynthetic genes encoding polyketides that are clustered together (Brown et al 1996;Keller and Hohn 1997;Hoffmeister and Keller 2007), which suggests that all genes that encode particular polyketide synthases are located adjacent to each other in the genome. However, the secondary metabolism of lichens at the molecular level is still unclear, and there have only been four studies conducted to date on these PKSs, namely one on three NR-PKSs of Xanthoparmelia semiviridis PKS (XsePKS1; Chooi et al 2008), Xanthoria elegans PKS (XePKS1; Brunauer et al 2009) and Dirinaria applanata PKS (DnPKS; Valarmathi et al 2009), and another on HR-PKS of Solorina crocea (SocPKS1; Gagunashvili et al 2009).…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of a non-reducing polyketide synthase gene from the lichen-forming fungus Usnea longissima

et al. 2011

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Usnea longissima has long been used as a traditional medicine in China, India, Turkey, Canada and Europe. This lichen can produce several bioactive compounds that primarily belong to the polyketide family. The enzymes responsible for the production of these compounds are the polyketide synthases, but the biosynthetic processes in lichens are still unclear. In this study, a cultured mycobiont of Usnea longissima was used to isolate and characterize a polyketide synthase gene (UlPKS1). Complete sequence information regarding UlPKS1 (6,468 bp) was obtained by screening a Fosmid genomic library using a 512-bp fragment corresponding to part of the ketosynthase (KS) domain. Sequence analysis of UlPKS1 suggested that it contained features of a non-reducing fungal type I PKS with a starter unit of ACP transacylase (SAT), ketosynthase (KS), product template (PT), acyl carrier protein (ACP) transacylase, acyltransferase (AT) and thioesterase (TE) domain, and had five intervening introns. The domain organization of UlPKS1 (SAT-KS-AT-PT-ACP-ACP-TE) was quite similar to that of aromatic PKSs, and phylogenetic analysis showed that UlPKS1 belonged to the clade of lichenized fungal non-reducing PKS. RT-PCR analyses revealed that the expression of UlPKS1 was downregulated by glycine and high concentrations of sorbitol, inositol and fructose and up-regulated by sucrose and glucose. Here, we introduce a non-reducing PKS gene in the lichen-forming fungus U. longissima, with a domain structure similar to the structure of orsellinic acid synthase A (OrsA) which is required for orsellinic acid biosynthesis in Aspergillus nidulans.

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Characterization of a non-reducing polyketide synthase gene from lichen Dirinaria applanata

Cited by 24 publications

References 36 publications

Isolation and characterization of a reducing polyketide synthase gene from the lichen-forming fungus Usnea longissima

Isolation and characterization of a reducing polyketide synthase gene from the lichen-forming fungus Usnea longissima

Three New Non-reducing Polyketide Synthase Genes from the Lichen-Forming Fungus Usnea longissima

Isolation and characterization of a non-reducing polyketide synthase gene from the lichen-forming fungus Usnea longissima

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