Biosynthesis and Accumulation of Ergoline Alkaloids in a Mutualistic Association between <i>Ipomoea asarifolia</i> (Convolvulaceae) and a Clavicipitalean Fungus

Markert, Astrid; Steffan, Nicola; Ploss, Kerstin; Hellwig, Sabine; Steiner, Ulrike; Drewke, Christel; Li, Shu-Ming; Boland, Wilhelm; Leistner, Eckhard

doi:10.1104/pp.108.116699

Cited by 80 publications

(77 citation statements)

References 64 publications

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“…In addition to 5-DMATS described in this study, several DMATSs using L-tryptophan as natural or best aromatic substrate with different regioselectivity have been studied biochemically in detail, e.g. the 4-DMATS FgaPT2 from A. fumigatus (20) and its orthologues MaPT from Malbranchea aurantiaca (50) and DmaW from a clavicipitalean fungus (51,52), the 6-DMATS IptA from Streptomyces sp. SN-593 (13), and the 7-DMATS from A. fumigatus (22).…”

Section: Discussionmentioning

confidence: 99%

Biochemical Characterization of Indole Prenyltransferases

Liu

Xie

et al. 2012

Journal of Biological Chemistry

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Background: Known indole prenyltransferases catalyzed regioselective prenylations at N-1, C-2, C-3, C-4, C-6, and C-7 of the indole ring. Results: Recombinant 5-DMATS was assayed with tryptophan and derivatives in the presence of DMAPP. Conclusion: 5-DMATS prenylated indole derivatives at C-5. Significance: 5-DMATS fills the last prenylation gap of indole derivatives and could be used as a potential catalyst for chemoenzymatic synthesis.

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Section: Discussionmentioning

confidence: 99%

Biochemical Characterization of Indole Prenyltransferases

Liu

Xie

et al. 2012

Journal of Biological Chemistry

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“…fumigatus exhibits 64%, 62%, and 55% sequence identity to the DMATs MaPT from M. aurantiaca (15), DmaW-Cs from a plantassociated clavicipitacean species (30), and DmaW-Cp from Claviceps purpurea P1 (31), respectively. These 3 enzymes catalyze the same reaction as FgaPT2.…”

Section: Comparison Of Dmatss From Different Fungal Species Fgapt2 Frommentioning

confidence: 99%

The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria

Metzger

Schall²,

Zocher³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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Ergot alkaloids are toxins and important pharmaceuticals that are produced biotechnologically on an industrial scale. The first committed step of ergot alkaloid biosynthesis is catalyzed by dimethylallyl tryptophan synthase (DMATS; EC 2.5.1.34). Orthologs of DMATS are found in many fungal genomes. We report here the x-ray structure of DMATS, determined at a resolution of 1.76 Å. A complex of DMATS from Aspergillus fumigatus with its aromatic substrate L-tryptophan and with an analogue of its isoprenoid substrate dimethylallyl diphosphate reveals the structural basis of this enzyme-catalyzed Friedel-Crafts reaction, which shows strict regiospecificity for position 4 of the indole nucleus of tryptophan as well as unusual independence of the presence of Mg 2؉ ions. The 3D structure of DMATS belongs to a rare ␤/␣ barrel fold, called prenyltransferase barrel, that was recently discovered in a small group of bacterial enzymes with no sequence similarity to DMATS. These bacterial enzymes catalyze the prenylation of aromatic substrates in the biosynthesis of secondary metabolites (i.e., a reaction similar to that of DMATS).EC 2.5.1.34 ͉ ergot alkaloids ͉ PT barrel ͉ ABBA prenyltransferase

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“…Tracer experiments have revealed that, in contrast with plants, not polyamines but Pro and homoserine are precursors of the lolines (Blankenship et al, 2005). Alkaloid-producing endophytes have also been described to occur in species of the Convolvulaceae (Steiner et al, 2006;Markert et al, 2008). As lolines in Argyreia might be products of as yet undiscovered fungal symbionts (Schardl et al, 2007), we excluded this species from our study and focus on the PA-producing species of the genus Ipomoea (sections Mina and Pharbitis) and Merremia in comparison with other PA-free species.…”

Section: Introductionmentioning

confidence: 99%

Evolution of Homospermidine Synthase in the Convolvulaceae: A Story of Gene Duplication, Gene Loss, and Periods of Various Selection Pressures

2013

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Homospermidine synthase (HSS), the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, is known to have its origin in the duplication of a gene encoding deoxyhypusine synthase. To study the processes that followed this gene duplication event and gave rise to HSS, we identified sequences encoding HSS and deoxyhypusine synthase from various species of the Convolvulaceae. We show that HSS evolved only once in this lineage. This duplication event was followed by several losses of a functional gene copy attributable to gene loss or pseudogenization. Statistical analyses of sequence data suggest that, in those lineages in which the gene copy was successfully recruited as HSS, the gene duplication event was followed by phases of various selection pressures, including purifying selection, relaxed functional constraints, and possibly positive Darwinian selection. Site-specific mutagenesis experiments have confirmed that the substitution of sites predicted to be under positive Darwinian selection is sufficient to convert a deoxyhypusine synthase into a HSS. In addition, analyses of transcript levels have shown that HSS and deoxyhypusine synthase have also diverged with respect to their regulation. The impact of protein–protein interaction on the evolution of HSS is discussed with respect to current models of enzyme evolution.

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Biosynthesis and Accumulation of Ergoline Alkaloids in a Mutualistic Association between Ipomoea asarifolia (Convolvulaceae) and a Clavicipitalean Fungus

Cited by 80 publications

References 64 publications

Biochemical Characterization of Indole Prenyltransferases

Biochemical Characterization of Indole Prenyltransferases

The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria

Evolution of Homospermidine Synthase in the Convolvulaceae: A Story of Gene Duplication, Gene Loss, and Periods of Various Selection Pressures

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