ADHII in Aspergillus nidulans Is Induced by Carbon Starvation Stress

Jones, I. G.; Fairhurst, Valerie; Sealy-Lewis, Heather M.

doi:10.1006/fgbi.2001.1250

Cited by 11 publications

(4 citation statements)

References 52 publications

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“…This result also indicates that alcB is not required for acetate repression because no significant derepression was observed. This result was not unexpected because it has been previously shown that alcB is induced during carbon starvation (Hunter et al 1996; Jones et al 2001), and Huisinga and Pugh (2004) reported that the SAGA complex of S. cerevisiae is involved in the up-regulation of genes in response to environmental stresses including carbon starvation. In addition to addressing whether the phenotype observed in solid medium containing acetate and allyl alcohol was due to the transcriptional regulation of alcB , this RT-qPCR, specifically the S conditions of this experiment, was also able to address whether the SAGA complex components AcdX and SptC were required for alcB regulation in response to carbon starvation.…”

Section: Resultssupporting

confidence: 57%

“…Because there are a number of alcohol dehydrogenases in A. nidulans , to allow interpretations to be drawn from this phenotypic test, relative transcription levels for alcA encoding alcohol dehydrogenase I, the enzyme required for ethanol metabolism (Lockington et al 1985), alcB encoding alcohol dehydrogenase II, induced during carbon starvation (Hunter et al 1996; Jones et al 2001), alcC encoding alcohol dehydrogenase III, the enzyme involved in anaerobic survival (Sealy-Lewis and Lockington 1984; McKnight et al 1985; Kelly et al 1990), and aldA encoding aldehyde dehydrogenase, the enzyme required for acetaldehyde metabolism (Pickett et al 1987), were determined using RT-qPCR.…”

Section: Resultsmentioning

confidence: 99%

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SAGA Complex Components and Acetate Repression inAspergillus nidulans

Georgakopoulos

Lockington²,

Kelly

2012

G3 Genes|Genomes|Genetics

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Alongside the well-established carbon catabolite repression by glucose and other sugars, acetate causes repression in Aspergillus nidulans. Mutations in creA, encoding the transcriptional repressor involved in glucose repression, also affect acetate repression, but mutations in creB or creC, encoding components of a deubiquitination system, do not. To understand the effects of acetate, we used a mutational screen that was similar to screens that uncovered mutations in creA, creB, and creC, except that glucose was replaced by acetate to identify mutations that were affected for repression by acetate but not by glucose. We uncovered mutations in acdX, homologous to the yeast SAGA component gene SPT8, which in growth tests showed derepression for acetate repression but not for glucose repression. We also made mutations in sptC, homologous to the yeast SAGA component gene SPT3, which showed a similar phenotype. We found that acetate repression is complex, and analysis of facA mutations (lacking acetyl CoA synthetase) indicates that acetate metabolism is required for repression of some systems (proline metabolism) but not for others (acetamide metabolism). Although plate tests indicated that acdX- and sptC-null mutations led to derepressed alcohol dehydrogenase activity, reverse-transcription quantitative real-time polymerase chain reaction showed no derepression of alcA or aldA but rather elevated induced levels. Our results indicate that acetate repression is due to repression via CreA together with metabolic changes rather than due to an independent regulatory control mechanism.

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Section: Resultssupporting

confidence: 57%

Section: Resultsmentioning

confidence: 99%

SAGA Complex Components and Acetate Repression inAspergillus nidulans

Georgakopoulos

Lockington²,

Kelly

2012

G3 Genes|Genomes|Genetics

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“…In the glucose condition, however, their expression exhibited no significant difference between Rut-C30 and Δ xyr1 (Table S5). In Aspergillus nidulans , an alcohol dehydrogenase (ADHII) was previously shown to be induced by carbon starvation stress [73]. We speculated that the transcription of these alcohol dehydrogenase genes could be sensitive to carbon starvation, but with no relationship to the existence of Xyr1.…”

Section: Resultsmentioning

confidence: 99%

RNA Sequencing Reveals Xyr1 as a Transcription Factor Regulating Gene Expression beyond Carbohydrate Metabolism

Chen

Zhang

et al. 2016

BioMed Research International

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Xyr1 has been demonstrated to be the main transcription activator of (hemi)cellulases in the well-known cellulase producer Trichoderma reesei. This study comprehensively investigates the genes regulated by Xyr1 through RNA sequencing to produce the transcription profiles of T. reesei Rut-C30 and its xyr1 deletion mutant (Δxyr1), cultured on lignocellulose or glucose. xyr1 deletion resulted in 467 differentially expressed genes on inducing medium. Almost all functional genes involved in (hemi)cellulose degradation and many transporters belonging to the sugar porter family in the major facilitator superfamily (MFS) were downregulated in Δxyr1. By contrast, all differentially expressed protease, lipase, chitinase, some ATP-binding cassette transporters, and heat shock protein-encoding genes were upregulated in Δxyr1. When cultured on glucose, a total of 281 genes were expressed differentially in Δxyr1, most of which were involved in energy, solute transport, lipid, amino acid, and monosaccharide as well as secondary metabolism. Electrophoretic mobility shift assays confirmed that the intracellular β-glucosidase bgl2, the putative nonenzymatic cellulose-attacking gene cip1, the MFS lactose transporter lp, the nmrA-like gene, endo T, the acid protease pepA, and the small heat shock protein hsp23 were probable Xyr1-targets. These results might help elucidate the regulation system for synthesis and secretion of (hemi)cellulases in T. reesei Rut-C30.

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“…The AdhIp encoded by the alcA gene is the physiological enzyme of ethanol catabolism [ 27 ]]; AdhIIp is encoded by the alcB gene [ 74 ], and AdhIIIp is encoded by the alcC gene [ 39 ]. The alcA gene is induced by ethanol and regulated by repression catabolism [ 75 ], and the alcB gene is induced by carbon starvation [ 38 ]. In general, in Aspergillus, the alc system is directed by two regulatory circuits controlling ethanol catabolism, the transcriptional activator AlcR and the repressor CreA [ 76 , 77 ].…”

Section: Regulation Of the Fungal Adhsmentioning

confidence: 99%

Fungal Alcohol Dehydrogenases: Physiological Function, Molecular Properties, Regulation of Their Production, and Biotechnological Potential

Gutiérrez-Corona,

González-Hernández,

Padilla-Guerrero

et al. 2023

Cells

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Fungal alcohol dehydrogenases (ADHs) participate in growth under aerobic or anaerobic conditions, morphogenetic processes, and pathogenesis of diverse fungal genera. These processes are associated with metabolic operation routes related to alcohol, aldehyde, and acid production. The number of ADH enzymes, their metabolic roles, and their functions vary within fungal species. The most studied ADHs are associated with ethanol metabolism, either as fermentative enzymes involved in the production of this alcohol or as oxidative enzymes necessary for the use of ethanol as a carbon source; other enzymes participate in survival under microaerobic conditions. The fast generation of data using genome sequencing provides an excellent opportunity to determine a correlation between the number of ADHs and fungal lifestyle. Therefore, this review aims to summarize the latest knowledge about the importance of ADH enzymes in the physiology and metabolism of fungal cells, as well as their structure, regulation, evolutionary relationships, and biotechnological potential.

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ADHII in Aspergillus nidulans Is Induced by Carbon Starvation Stress

Cited by 11 publications

References 52 publications

SAGA Complex Components and Acetate Repression inAspergillus nidulans

SAGA Complex Components and Acetate Repression inAspergillus nidulans

RNA Sequencing Reveals Xyr1 as a Transcription Factor Regulating Gene Expression beyond Carbohydrate Metabolism

Fungal Alcohol Dehydrogenases: Physiological Function, Molecular Properties, Regulation of Their Production, and Biotechnological Potential

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