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  • 1
    Electronic Resource
    Electronic Resource
    Mitochondrial β-oxidation in Aspergillus nidulans (2004)
    Oxford, UK : Blackwell Publishing Ltd.
    Molecular microbiology 54 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: β-Oxidation (β-ox) occurs exclusively in the peroxisomes of Saccharomyces cerevisiae and other yeasts, leading to the supposition that fungi lack mitochondrial β-ox. Here we present unequivocal evidence that the filamentous fungus Aspergillus nidulans houses both peroxisomal and mitochondrial β-ox. While growth of a peroxisomal β-ox disruption mutant (ΔfoxA) was eliminated on a very long-chain fatty acid (C22:1), growth was only partially impeded on a long-chain fatty acid (C18:1) and was not affected at all on short chain (C4–C6) fatty acids. In contrast, growth of a putative enoyl-CoA hydratase mutant (ΔechA) was abolished on short-chain and severely restricted on long- and very long-chain fatty acids. Furthermore fatty acids inhibited growth of the ΔechA mutant but not the ΔfoxA mutant in the presence of an alternate carbon source (lactose). Disruption of echA led to a 28-fold reduction in 2-butenoyl-CoA hydratase activity in a preparation of organelles. EchA was also required for growth on isoleucine and valine. The subcellular localization of the FoxA and EchA proteins was confirmed through the use of red and green fluorescent protein fusions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04340.x
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  • 2
    Electronic Resource
    Electronic Resource
    Blockage of methylcitrate cycle inhibits polyketide production in Aspergillus nidulans (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 52 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Aspergillus nidulans produces the polyketide toxin sterigmatocystin (ST) of which the biosynthetic and pathway specific regulatory genes compose a stc gene cluster. A previous mutagenesis screen identified 23 mutants defective in production of ST. Five mutants constitute a single locus. Genetic complementation and sequencing analysis revealed the mutant locus to be mcsA encoding methylcitrate synthase that converts propionyl-CoA to methylcitrate. Feeding downstream products of methylcitrate synthase, methylcitrate and pyruvate, did not restore ST production in mcsA mutants, indicating that loss of methylcitrate cycle products is not the cause of the ST defect. However, propionate, a precursor for propionyl-CoA, inhibited ST production and induced transcription of mcsA in the wild type. Furthermore, propionate impaired formation of two polyketide spore pigments whereas overexpression of mcsA relieved inhibition of ST production by propionate. Transcription analyses revealed that disruption of mcsA did not affect expression of the specialized fatty acid synthase genes (stcJ and stcK) or polyketide synthase gene (stcA) required for formation of norsolorinic acid (NOR), the first stable intermediate in the ST biosynthetic pathway. Feeding studies showed that NOR but not hexanoic acid (the fatty acid produced by StcJ/StcK and primer unit of StcA) or malonate (source of the extender unit of StcA) restored ST production in the mcsA mutant. We hypothesize that excess buildup of propionyl-CoA in mcsA mutants interferes with polyketide synthase activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.03994.x
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  • 3
    Electronic Resource
    Electronic Resource
    Requirement of spermidine for developmental transitions in Aspergillus nidulans (2002)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 46 (2002), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Deletion of the spermidine synthase gene in the fungus Aspergillus nidulans results in a strain, ΔspdA, which requires spermidine for growth and accumulates putrescine as the sole polyamine. Vegetative growth but not sporulation or sterigmatocystin production is observed when ΔspdA is grown on media supplemented with 0.05–0.10 mM exogenous spermidine. Supplementation of ΔspdA with ≥ 0.10 mM spermidine restores sterigmatocystin production and ≥ 0.50 mM spermidine produces a phenotype with denser asexual spore production and decreased radial hyphal growth compared with the wild type. ΔspdA spores germinate in unsupplemented media but germ tube growth ceases after 8 h upon which time the spores swell to approximately three times their normal diameter. Hyphal growth is resumed upon addition of 1.0 mM spermidine. Suppression of a G protein signalling pathway could not force asexual sporulation and sterigmatocystin production in ΔspdA strains grown in media lacking spermidine but could force both processes in ΔspdA strains supplemented with 0.05 mM spermidine. These results show that increasing levels of spermidine are required for the transitions from (i) germ tube to hyphal growth and (ii) hyphal growth to tissue differentiation and secondary metabolism. Suppression of G protein signalling can over-ride the spermidine requirement for the latter but not the former transition.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2002.03201.x
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  • 4
    Electronic Resource
    Electronic Resource
    A peanut seed lipoxygenase responsive to Aspergillus colonization (2000)
    Springer
    Plant molecular biology 42 (2000), S. 689-701 
    Details
    ISSN: 1573-5028
    Keywords: Arachis hypogaea ; Aspergillus parasiticus ; lipoxygenase ; plant defense gene ; plant/microbe interaction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several lines of evidence have indicated that lipoxygenase enzymes (LOX) and their products, especially 9S- and 13S-hydroperoxy fatty acids, could play a role in the Aspergillus/seed interaction. Both hydroperoxides exhibit sporogenic effects on Aspergillus spp. (Calvo, A., Hinze, L., Gardner, H.W. and Keller, N.P. 1999. Appl. Environ. Microbiol. 65: 3668–3673) and differentially modulate aflatoxin pathway gene transcription (Burow, G.B., Nesbitt, T.C., Dunlap, J. and Keller, N.P. 1997. Mol. Plant-Microbe Interact. 10: 380–387). To examine the role of seed LOXs at the molecular level, a peanut (Arachis hypogaea L.) seed gene, PnLOX1, was cloned and characterized. Analysis of nucleotide sequence suggests that PnLOX1 encodes a predicted 98 kDa protein highly similar in sequence and biochemical properties to soybean LOX2. The full-length PnLOX1 cDNA was subcloned into an expression vector to determine the type(s) of hydroperoxide products the enzyme produces. Analysis of the oxidation products of PnLOX1 revealed that it produced a mixture of 30% 9S-HPODE (9S-hydroperoxy-10E, 12Z-octadecadienoic acid) and 70% 13S-HPODE (13S-hydroperoxy-9Z, 11E-octadecadienoic acid) at pH 7. PnLOX1 is an organ-specific gene which is constitutively expressed in immature cotyledons but is highly induced by methyl jasmonate, wounding and Aspergillus infections in mature cotyledons. Examination of HPODE production in infected cotyledons suggests PnLOX1 expression may lead to an increase in 9S-HPODE in the seed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006361305703
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