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Cloning and sequence characterization of a non-reducing polyketide synthase gene from the lichen Xanthoparmelia semiviridis

Chooi, Yit-Heng; Stalker, David M; Davis, Meryl A; Fujii, Isao; Elix, John; Louwhoff, Simone; Lawrie, Ann C

Description

Lichens produce a diverse array of secondary metabolites that have shown various biological activities. Of particular interest are the coupled phenolics that originate from polyketide pathways, such as depsides, depsidones and usnic acids, which are produced almost solely by lichens. Based on the presumed catalytic domains required for the synthesis of the key intermediates β-orsellinic acid and methylphloroacetophenone, two pairs of degenerate primers were designed to target specifically the...[Show more]

dc.contributor.authorChooi, Yit-Heng
dc.contributor.authorStalker, David M
dc.contributor.authorDavis, Meryl A
dc.contributor.authorFujii, Isao
dc.contributor.authorElix, John
dc.contributor.authorLouwhoff, Simone
dc.contributor.authorLawrie, Ann C
dc.date.accessioned2015-12-10T22:27:21Z
dc.identifier.issn0953-7562
dc.identifier.urihttp://hdl.handle.net/1885/54166
dc.description.abstractLichens produce a diverse array of secondary metabolites that have shown various biological activities. Of particular interest are the coupled phenolics that originate from polyketide pathways, such as depsides, depsidones and usnic acids, which are produced almost solely by lichens. Based on the presumed catalytic domains required for the synthesis of the key intermediates β-orsellinic acid and methylphloroacetophenone, two pairs of degenerate primers were designed to target specifically the β-ketoacylsynthase (KS) and C-methyltransferase (CMeT) domains of fungal non-reducing polyketide synthase (NR-PKS) genes with CMeT domains. These primers were used to explore the genome of the lichen Xanthoparmelia semiviridis, which produces β-orcinol depsidones and usnic acid. One of the two KS domains amplified from genomic DNA of field-collected X. semiviridis was used as a probe to recover the candidate PKS gene. A 13 kb fragment containing an intact putative PKS gene (xsepks1) of 6555 bp was recovered from a partial genomic library. The inferred amino acid sequence indicated that xsepks1 encodes a protein of 2164 amino acids and contains KS, acyltransferase (AT), acyl carrier protein (ACP) and CMeT domains as expected. This demonstrated a successful strategy for targeting non-reducing PKS genes with CMeT domains. Integration of the 5′ fragment of xsepks1, including the native promoter, into Aspergillus nidulans by cotransformation resulted in the transcription of the 5′ xsepks1 and the splicing of a 63 bp intron, suggesting that A. nidulans could be a suitable heterologous host for xsepks1 expression.
dc.publisherElsevier
dc.sourceMycological Research
dc.subjectKeywords: fungal protein; polyketide synthase; clone; enzyme activity; gene; genetic analysis; genome; lichen; secondary metabolite; article; Ascomycetes; Aspergillus nidulans; biosynthesis; chemistry; classification; enzymology; genetics; high performance liquid c Chondropsis; Depsidones; Parmeliaceae; Secondary metabolites; Usnic acid
dc.titleCloning and sequence characterization of a non-reducing polyketide synthase gene from the lichen Xanthoparmelia semiviridis
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume112
dc.date.issued2008
local.identifier.absfor060310 - Plant Systematics and Taxonomy
local.identifier.absfor060107 - Enzymes
local.identifier.absfor060505 - Mycology
local.identifier.ariespublicationu4005981xPUB293
local.identifier.ariespublicationu4956746xPUB355
local.type.statusPublished Version
local.contributor.affiliationChooi, Yit-Heng, RMIT University
local.contributor.affiliationStalker, David M, RMIT University
local.contributor.affiliationDavis, Meryl A, University of Melbourne
local.contributor.affiliationFujii, Isao, University of Tokyo
local.contributor.affiliationElix, John, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationLouwhoff, Simone, Royal Botanic Gardens Melbourne
local.contributor.affiliationLawrie, Ann C, RMIT University
local.description.embargo2037-12-31
local.bibliographicCitation.issue2
local.bibliographicCitation.startpage147
local.bibliographicCitation.lastpage161
local.identifier.doi10.1016/j.mycres.2007.08.022
local.identifier.absseo860803 - Human Pharmaceutical Treatments (e.g. Antibiotics)
dc.date.updated2015-12-09T09:40:01Z
local.identifier.scopusID2-s2.0-39749125473
local.identifier.thomsonID000255080400004
CollectionsANU Research Publications

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