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A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation [2009]

ABSTRACT: Experience 1: 59A vs. 59A NADPH Bdh100mM

ORGANISM(S): Saccharomyces cerevisiae

PROVIDER: GSE34808 | GEO | 2012/04/01

SECONDARY ACCESSION(S): PRJNA156289

REPOSITORIES: GEO

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A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation [2010]

Project description:Experience 2: 59A vs. 59A NADH Bdh200 mM, 59A NADPH Bdh200mM and 59A NADPH Bdh300 mM

2012-04-01 | GSE34809 | GEO

A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation [2009]

Project description:Experience 1: 59A vs. 59A NADPH Bdh100mM Analysis used RNA samples of three independent replicates by strain extracted from cells harvested at mid-exponential phase of oenological fermentation

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A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation [2010]

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A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation

Project description:This SuperSeries is composed of the following subset Series: GSE34808: A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation [2009] GSE34809: A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation [2010] Refer to individual Series

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A transcriptomic analysis of the response of Saccharomyces cerevisiae to increases in NADPH oxidation

Project description:This SuperSeries is composed of the SubSeries listed below.

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The reducing equivalent NADPH dictates histone acetylation via direct inactivation of HDAC3

Project description:NADPH has been long well-recognized as a key cofactor for antioxidant defense and reductive biosynthesis. Here we report a metabolism-independent function of NADPH in modulating epigenetic status and transcription. We found that reduction of cellular NADPH levels by silencing malic enzyme (ME) or G6PD impairs global histone acetylation and transcription in both adipocytes and tumor cells. These effects can be reversed by supplementation of exogenous NADPH or inhibition of histone deacetylase 3 (HDAC3). Mechanistically, NADPH or inhibition of histone deacetylase 3 (HDAC3). Mechanistically,NADPH directly interacts with HDAC3 and interrupts the association between HDAC3 and its co-activator Ncor2 (SMRT) or Ncor1, thereby impairs HDAC3 activation. Interestingly, it appears that NADPH and Ins(1,4,5,6)P4 bind to the same domains on HDAC3, and NADPH has relatively higher affinity towards HDAC3. Thus, while Ins(1,4,5,6)P4 acts as an ‘intermolecular glue’, NADPH may function as a HDAC3-Ncor assembly inhibitor. Collectively, our findings uncovered a previous unidentified and metabolism-independent role of NADPH in controlling epigenetic change and gene expression by acting as an endogenous inhibitor of HDAC3.

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High-level furfural resistance in S. cerevisiae is based on NADPH-dependent reduction by at least two oxireductases

Project description:Resistance of Saccharomyces cerevisiae to high furfural concentration is based on NADPH-dependent reduction by at least two oxireductases. Biofuels derived from lignocellulosic biomass hold promises for a sustainable fuel economy, but several problems hamper their economical feasibility. One important problem is the presence of toxic compounds in processed lignocellulosic hydrolysates with furfural as a key toxin. While Saccharomyces cerevisiae has some intrinsic ability to reduce furfural to the less toxic furfuryl alcohol, higher resistance is necessary for process conditions. By comparing an evolved, furfural resistant strain and its parent in micro-aerobic, glucose-limited chemostats at increasing furfural challenge, we elucidate key mechanism and the molecular basis of both natural and high-level furfural resistance. At lower furfural concentrations, NADH-dependent oxireductases are the main defence mechanism. At concentrations above 15 mM, however, [1-13C]-flux and global array-based transcript analysis demonstrated that the NADPH-generating flux through pentose-phosphate pathway increases and that NADPH-dependent oxireductases became the major resistance mechanism. The transcript analysis further revealed that iron transmembrane transport is up-regulated in response to furfural. While these responses occur in both strains, high-level resistance in the evolved strain was based on strong induction of ADH7, the uncharacterised ORF YKL071W and 4 further, likely NADPH-dependent oxireductases. By overexpressing the ADH7 gene and the ORF YKL071W, we inverse engineered significantly increased furfural resistance in the parent strain, thereby demonstrating these two enzymes to be key elements of the resistance phenotype.

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