Biodiversity and evolution of primary carbon metabolism in Aspergillus nidulans and other Aspergillus spp.

Flipphi, Michel; Sun, Jibin; Robellet, Xavier; Karaffa, Levente; Fekete, Erzsébet; Zeng, An‐Ping; Kubicek, Christian P.

doi:10.1016/j.fgb.2008.07.018

Cited by 100 publications

(94 citation statements)

References 103 publications

(97 reference statements)

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“…This other route showed oxidation to galactitol, but the subsequent steps were unidentified. It was suggested that the pathway proceeds via L-sorbose and D-sorbitol or even via sorbose 6-phosphate and D-tagatose 1,6-bisphosphate (24). A. nidulans has, in addition to GalX, an additional transcriptional regulator, GalR, which is unique among ascomycetes (19).…”

mentioning

confidence: 99%

l-xylo-3-Hexulose Reductase Is the Missing Link in the Oxidoreductive Pathway for d-Galactose Catabolism in Filamentous Fungi

Mojžita

Herold

Metz

et al. 2012

Journal of Biological Chemistry

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Background:There is an oxidoreductive D-galactose pathway in filamentous fungi. Results:We identified an L-xylo-3-hexulose reductase that produces D-sorbitol and that is part of this pathway. Conclusion: This L-xylo-3-hexulose reductase is the missing link in the oxidoreductive D-galactose pathway. Significance: The alternative pathway for D-galactose catabolism in filamentous fungi is elucidated.

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confidence: 99%

l-xylo-3-Hexulose Reductase Is the Missing Link in the Oxidoreductive Pathway for d-Galactose Catabolism in Filamentous Fungi

Mojžita

Herold

Metz

et al. 2012

Journal of Biological Chemistry

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“…There are related genes in other Aspergillus spp. with additional copies in the three sequenced A. niger strains (16,44). These additional putative citrate synthases are not present in either N. crassa or Magnaporthe grisea (44).…”

Section: Cap655041)mentioning

confidence: 92%

“…As fungal pathogens establish infection they must adapt their utilization of carbon sources to the substrates present in the new environment of the host cells (reviewed in reference 6). With many of the fungal genomes available, the number of genes encoding enzymes and transporters potentially involved in central metabolism has become apparent and is greater than might have been anticipated (for example, see reference 16). Deciphering this complexity requires not only genome-wide studies but also detailed studies of individual genes encoding these proteins in order to determine their regulation and the cellular localization of the proteins, as well as their roles in metabolism and development.…”

mentioning

confidence: 99%

Metabolic and Developmental Effects Resulting from Deletion of thecitAGene Encoding Citrate Synthase in Aspergillus nidulans

Murray

Hynes

2010

Eukaryot Cell

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Citrate synthase is a central activity in carbon metabolism. It is required for the tricarboxylic acid (TCA) cycle, respiration, and the glyoxylate cycle. In Saccharomyces cerevisiae and Arabidopsis thaliana, there are mitochondrial and peroxisomal isoforms encoded by separate genes, while in Aspergillus nidulans, a single gene, citA, encodes a protein with predicted mitochondrial and peroxisomal targeting sequences (PTS). Deletion of citA results in poor growth on glucose but not on derepressing carbon sources, including those requiring the glyoxylate cycle. Growth on glucose is restored by a mutation in the creA carbon catabolite repressor gene. Methylcitrate synthase, required for propionyl-coenzyme A (CoA) metabolism, has previously been shown to have citrate synthase activity. We have been unable to construct the mcsA⌬ citA⌬ double mutant, and the expression of mcsA is subject to CreA-mediated carbon repression. Therefore, McsA can substitute for the loss of CitA activity. Deletion of citA does not affect conidiation or sexual development but results in delayed conidial germination as well as a complete loss of ascospores in fruiting bodies, which can be attributed to loss of meiosis. These defects are suppressed by the creA204 mutation, indicating that McsA activity can substitute for the loss of CitA. A mutation of the putative PTS1-encoding sequence in citA had no effect on carbon source utilization or development but did result in slower colony extension arising from single conidia or ascospores. CitA-green fluorescent protein (GFP) studies showed mitochondrial localization in conidia, ascospores, and hyphae. Peroxisomal localization was not detected. However, a very low and variable detection of punctate GFP fluorescence was sometimes observed in conidia germinated for 5 h when the mitochondrial targeting sequence was deleted.There has been increased interest in primary carbon metabolism in fungi in recent years. There are two main reasons for this. As fungal pathogens establish infection they must adapt their utilization of carbon sources to the substrates present in the new environment of the host cells (reviewed in reference 6). With many of the fungal genomes available, the number of genes encoding enzymes and transporters potentially involved in central metabolism has become apparent and is greater than might have been anticipated (for example, see reference 16). Deciphering this complexity requires not only genome-wide studies but also detailed studies of individual genes encoding these proteins in order to determine their regulation and the cellular localization of the proteins, as well as their roles in metabolism and development. Here we report molecular genetic analysis of the citA gene encoding citrate synthase (EC 4.1.3.7), a central enzyme of carbon metabolism, in the filamentous ascomycete Aspergillus nidulans.Citrate synthase is required for the formation of citrate from acetyl-coenzyme A (CoA) and oxaloacetate in the tricarboxylic acid (TCA) cycle and is therefore necessary for respirat...

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“…As part of a community-wide effort to curate, correct and update the automated gene annotation of the Aspergillus nidulans genome sequences [40], we previously identified the (putative) structural genes of the Leloir pathway of D-galactose metabolism in nine species of Aspergillus [17]. Aspergillus is the sister genus of Penicillium in the family of the Aspergillaceae [22] comprizing several hundred species including fungi widely used in the fermentation industry such as A. niger and A. oryzae, the opportunistic human pathogen A. fumigatus and the genetic model A. nidulans.…”

Section: Acta Biologica Hungarica 67 2016mentioning

confidence: 99%

“…The weakly expressed A. nidulans gene for the paralog enzyme, ugeB, had been identified in an earlier work [32]. We included its P. chrysogenum ortholog as well as three additional autoannotated epimerase genes structurally related to A. nidulans loci AN0746 and AN3119 [17] in our current study to assess their possible role in Leloir catabolism of D-galactose next to ugeA. The mined P. chrysogenum genes for galactokinase (galE) and galactose-1-phosphate uridylyl transferase (galD) are the orthologs of the A. nidulans genes that are allelic to well-characterized, classically selected galactoseutilization mutations called galE9 and galD5, respectively [1,35].…”

Section: Growth Of Penicillium Chrysogenum On D-galactosementioning

confidence: 99%

D-galactose catabolism inPenicillium chrysogenum: Expression analysis of the structural genes of the Leloir pathway

Jónás

Fekete

Németh

et al. 2016

Acta Biologica Hungarica

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In this study, we analyzed the expression of the structural genes encoding the five enzymes comprising the Leloir pathway of D-galactose catabolism in the industrial cell factory Penicillium chrysogenum on various carbon sources. The genome of P. chrysogenum contains a putative galactokinase gene at the annotated locus Pc13g10140, the product of which shows strong structural similarity to yeast galactokinase that was expressed on lactose and D-galactose only. The expression profile of the galactose-1-phosphate uridylyl transferase gene at annotated locus Pc15g00140 was essentially similar to that of galactokinase. This is in contrast to the results from other fungi such as Aspergillus nidulans, Trichoderma reesei and A. niger, where the ortholog galactokinase and galactose-1-phosphate uridylyl transferase genes were constitutively expressed. As for the UDP-galactose-4-epimerase encoding gene, five candidates were identified. We could not detect Pc16g12790, Pc21g12170 and Pc20g06140 expression on any of the carbon sources tested, while for the other two loci (Pc21g10370 and Pc18g01080) transcripts were clearly observed under all tested conditions. Like the 4-epimerase specified at locus Pc21g10370, the other two structural Leloir pathway genes -UDP-glucose pyrophosphorylase (Pc21g12790) and phosphoglucomutase (Pc18g01390) -were expressed constitutively at high levels as can be expected from their indispensable function in fungal cell wall formation.

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Biodiversity and evolution of primary carbon metabolism in Aspergillus nidulans and other Aspergillus spp.

Cited by 100 publications

References 103 publications

l-xylo-3-Hexulose Reductase Is the Missing Link in the Oxidoreductive Pathway for d-Galactose Catabolism in Filamentous Fungi

l-xylo-3-Hexulose Reductase Is the Missing Link in the Oxidoreductive Pathway for d-Galactose Catabolism in Filamentous Fungi

Metabolic and Developmental Effects Resulting from Deletion of thecitAGene Encoding Citrate Synthase in Aspergillus nidulans

D-galactose catabolism inPenicillium chrysogenum: Expression analysis of the structural genes of the Leloir pathway

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