Carbon source-dependent transcriptional regulation of the mitochondrial glycerol-3-phosphate dehydrogenase gene,<i>GUT2</i>, from<i>Saccharomyces cerevisiae</i>

Grauslund, Morten; Rønnow, Birgitte

doi:10.1139/w00-105

Cited by 44 publications

(31 citation statements)

References 25 publications

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“…Gut2p (glycerol 3-phosphate dehydrogenase isozyme 2), which was detected only under BFC, oxidizes glycerol 3-phosphate to dihydroxy-acetone-phosphate in the glycerol degradation pathway. Gut2p expression is repressed by glucose and derepressed by nonfermentable carbon sources in a Snf1p, Rsf1p, Hap2/ 3/4/5/7 complex dependent manner (Tadi et al, 1999;Grauslund and Ronnow, 2000;Pahlman et al, 2002;Lu et al, 2003). Besides effecting glycerol degradation, Gut2p plays a central role in maintaining redox balance between NAD þ and NADH under aerobic conditions in combination with the dehydrogenases Nde1p and Nde2p, and the lactate dehydrogenases Dld1p and Cyb2p (Grandier-Vazeille et al, 2001)dCyb2p was also detected under BFC (see table in the Supplementary Material).…”

Section: Discussionmentioning

confidence: 99%

Proteins involved in wine aroma compounds metabolism by a Saccharomyces cerevisiae flor-velum yeast strain grown in two conditions

et al. 2015

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Section: Discussionmentioning

confidence: 99%

Proteins involved in wine aroma compounds metabolism by a Saccharomyces cerevisiae flor-velum yeast strain grown in two conditions

et al. 2015

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“…It is possible that other functional shuttle components may compensate for the disabled ones under normal growth conditions (2% glucose). Under growth conditions that favor glycolysis, such as growth in the presence of excess glucose, expression of the malate-aspartate shuttle components and tricarbolic acid cycle enzymes are repressed (Minard and McAlister-Henn 1992;Ferea et al 1999;Grauslund and Ronnow 2000). These glucose-repressed genes resume gene expression when glucose is depleted in the growth media (derepression).…”

Section: Overexpression Of the Nadh Shuttle Components Function In Thmentioning

confidence: 99%

The malate–aspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast

Easlon¹,

Tsang²,

Skinner³

et al. 2008

Genes Dev.

133

118

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Recent studies suggest that increased mitochondrial metabolism and the concomitant decrease in NADH levels mediate calorie restriction (CR)-induced life span extension. The mitochondrial inner membrane is impermeable to NAD (nicotinamide adenine dinucleotide, oxidized form) and NADH, and it is unclear how CR relays increased mitochondrial metabolism to multiple cellular pathways that reside in spatially distinct compartments. Here we show that the mitochondrial components of the malate-aspartate NADH shuttle (Mdh1 [malate dehydrogenase] and Aat1 [aspartate amino transferase]) and the glycerol-3-phosphate shuttle (Gut2, glycerol-3-phosphate dehydrogenase) are novel longevity factors in the CR pathway in yeast. Overexpressing Mdh1, Aat1, and Gut2 extend life span and do not synergize with CR. Mdh1 and Aat1 overexpressions require both respiration and the Sir2 family to extend life span. The mdh1⌬aat1⌬ double mutation blocks CR-mediated life span extension and also prevents the characteristic decrease in the NADH levels in the cytosolic/nuclear pool, suggesting that the malate-aspartate shuttle plays a major role in the activation of the downstream targets of CR such as Sir2. Overexpression of the NADH shuttles may also extend life span by increasing the metabolic fitness of the cells. Together, these data suggest that CR may extend life span and ameliorate age-associated metabolic diseases by activating components of the NADH shuttles.[Keywords: Calorie restriction (CR); Sir2; aging; NADH shuttles; respiration; metabolism] Supplemental material is available at http://www.genesdev.org.

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“…Gut2p is localized in the inner mitochondrial membrane, where it oxidizes glycerol-3-phosphate to dihydroxyacetone phosphate. Together with Gut1p, it acts as a glycerol-3-phosphate shuttle that is responsible for oxidation of NADH under aerobic conditions [40]. It has been proposed that under anaerobiosis the aldehyde dehydrogenase Adh3p, collaborates together with the fumarate reductase and the glycerol-3-phosphate dehydrogenase to maintain redox balance [41].…”

Section: Mitochondrial Membrane Protein Complex Formation And/or Stabmentioning

confidence: 99%

A three‐way proteomics strategy allows differential analysis of yeast mitochondrial membrane protein complexes under anaerobic and aerobic conditions

et al. 2009

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To investigate the effect of anaerobiosis on the Saccharomyces cerevisiae mitochondrial proteome and the formation of respiratory chain and other protein complexes, we analyzed mitochondrial protein extracts that were enriched from lysates of aerobic and anaerobic steady-state chemostat cultures. We chose an innovative approach in which native mitochondrial membrane protein complexes were separated by 1-D blue native PAGE, which was combined with quantitative analysis of each complex subunit using stable isotope labeling. LC-FT(ICR)-MS/MS analysis was applied to identify and quantify the mitochondrial proteins. In addition, to establish if changes in mitochondrial complex composition occurred under anaerobiosis, we investigated the 1-D blue native PAGE protein migration patterns by Pearson correlation analysis. Surprisingly, we discovered that under anaerobic conditions, where the yeast respiratory chain is not active, the respiratory chain supercomplexes, such as complex V dimer, complex (III) 2 (IV) 2 and complex (III) 2 (IV) were still present, although at reduced levels. Pearson correlation analysis showed that the composition of the mitochondrial complexes was unchanged under aerobic or anaerobic conditions, with the exception of complex II. In addition, this latter approach allowed screening for possible novel complex interaction partners, since for example protein Aim38p, with a yet unknown function, was identified as a possible component of respiratory chain complex IV.

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Carbon source-dependent transcriptional regulation of the mitochondrial glycerol-3-phosphate dehydrogenase gene,GUT2, fromSaccharomyces cerevisiae

Cited by 44 publications

References 25 publications

Proteins involved in wine aroma compounds metabolism by a Saccharomyces cerevisiae flor-velum yeast strain grown in two conditions

Proteins involved in wine aroma compounds metabolism by a Saccharomyces cerevisiae flor-velum yeast strain grown in two conditions

The malate–aspartate NADH shuttle components are novel metabolic longevity regulators required for calorie restriction-mediated life span extension in yeast

A three‐way proteomics strategy allows differential analysis of yeast mitochondrial membrane protein complexes under anaerobic and aerobic conditions

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