Physiological role of soluble fumarate reductase in redox balancing during anaerobiosis in Saccharomyces cerevisiae

Enomoto, K

doi:10.1016/s0378-1097(02)00918-7

Cited by 22 publications

(30 citation statements)

References 21 publications

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“…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]. We detected down-regulation of Gut2p, which points to reduced participation of the glycerol shuttle in the control of the NAD/ NADH redox balance during anaerobiosis.…”

Section: Mitochondrial Membrane Protein Complex Formation And/or Stabmentioning

confidence: 64%

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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Section: Mitochondrial Membrane Protein Complex Formation And/or Stabmentioning

confidence: 64%

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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“…gpd1 ϩ , glycerol-3-phosphate dehydrogenase, and adh1 ϩ , alcohol dehydrogenase, were upregulated anaerobically independently of Sre1p and have been suggested to be involved in the reoxidizing of NADH in S. cerevisiae under anaerobic conditions (4). Another proposed mechanism for regulating NADH/NAD ϩ redox balance during anaerobiosis is through fumarate reductase (11). Interestingly, osm1 ϩ (SPAC17A2.05), encoding a predicted fumarate reductase, was highly upregulated by Sre1p during anaerobiosis (Table 1 and Fig.…”

mentioning

confidence: 99%

“…Fumarate reductase converts fumarate to succinate and requires FADH 2 or FMNH 2 but not NADH. Thus, another enzyme likely oxidizes NADH while reducing the oxidized flavin generated from fumarate reductase to maintain the NADH/NAD ϩ redox balance (11). Indeed, an uncharacterized Sre1p-dependent anaerobically upregulated gene, SPBC23G7.10c, contains an NADH-dependent flavin oxidoreductase domain coding sequence and could potentially serve this function.…”

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confidence: 99%

Sterol Regulatory Element Binding Protein Is a Principal Regulator of Anaerobic Gene Expression in Fission Yeast

Todd

Stewart

Burg

et al. 2006

Molecular and Cellular Biology

161

240

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Fission yeast sterol regulatory element binding protein (SREBP), called Sre1p, functions in an oxygensensing pathway to allow adaptation to fluctuating oxygen concentrations. The Sre1p-Scp1p complex responds to oxygen-dependent sterol synthesis as an indirect measure of oxygen availability. To examine the role of Sre1p in anaerobic gene expression in Schizosaccharomyces pombe, we performed transcriptional profiling experiments after a shift to anaerobic conditions for 1.5 h. Of the 4,940 genes analyzed, expression levels of 521 (10.5%) and 686 (13.9%) genes were significantly increased and decreased, respectively, under anaerobic conditions. Sre1p controlled 68% of genes induced >2-fold. Oxygen-requiring biosynthetic pathways for ergosterol, heme, sphingolipid, and ubiquinone were primary targets of Sre1p. Induction of glycolytic genes and repression of mitochondrial oxidative phosphorylation genes largely did not require Sre1p. Using chromatin immunoprecipitation, we demonstrated that Sre1p acts directly at target gene promoters and stimulates its own transcription under anaerobic conditions. sre1 ؉ promoter analysis identified two DNA elements that are both necessary and sufficient for oxygen-dependent, Sre1p-dependent transcription. Interestingly, these elements are homologous to sterol regulatory elements bound by mammalian SREBP, highlighting the evolutionary conservation between Sre1p and SREBP. We conclude that Sre1p is a principal activator of anaerobic gene expression, upregulating genes required for nonrespiratory oxygen consumption.

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“…The FRDs of several Shewanella species, S. cerevisiae, M. thermoautotrophicus, and T. brucei belong to this group. These enzymes are different from the H. thermophilus FRD in their functions and, in some cases, their electron donors (5,8,12,15,18,20,46).…”

Section: Discussionmentioning

confidence: 89%

“…The two FRDs of S. cerevisiae irreversibly reduce fumarate to succinate, using FADH 2 , FMNH 2 , or reduced riboflavin as electron donors. These enzymes are suggested to be involved in the maintenance of the intracellular redox balance under anaerobic conditions (8,15). The genes encoding two FRDs from the protozoan parasite T. brucei were studied and provide the first reports of soluble, NADH-dependent FRDs (5,12).…”

mentioning

confidence: 99%

A Soluble NADH-Dependent Fumarate Reductase in the Reductive Tricarboxylic Acid Cycle of Hydrogenobacter thermophilus TK-6

et al. 2008

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Fumarate reductase (FRD) is an enzyme that reduces fumarate to succinate. In many organisms, it is bound to the membrane and uses electron donors such as quinol. In this study, an FRD from a thermophilic chemolithoautotrophic bacterium, Hydrogenobacter thermophilus TK-6, was purified and characterized. FRD activity using NADH as an electron donor was not detected in the membrane fraction but was found in the soluble fraction. The purified enzyme was demonstrated to be a novel type of FRD, consisting of five subunits. One subunit showed high sequence identity to the catalytic subunits of known FRDs. Although the genes of typical FRDs are assembled in a cluster, the five genes encoding the H. thermophilus FRD were distant from each other in the genome. Furthermore, phylogenetic analysis showed that the H. thermophilus FRD was located in a distinct position from those of known soluble FRDs. This is the first report of a soluble NADH-dependent FRD in Bacteria and of the purification of a FRD that operates in the reductive tricarboxylic acid cycle.

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Physiological role of soluble fumarate reductase in redox balancing during anaerobiosis in Saccharomyces cerevisiae

Cited by 22 publications

References 21 publications

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

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

Sterol Regulatory Element Binding Protein Is a Principal Regulator of Anaerobic Gene Expression in Fission Yeast

A Soluble NADH-Dependent Fumarate Reductase in the Reductive Tricarboxylic Acid Cycle of Hydrogenobacter thermophilus TK-6

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