One of the Fumarate Reductase Isoenzymes fromSaccharomyces cerevisiaeIs Encoded by theOSM1Gene

Muratsubaki, Haruhiro; Enomoto, Keiichiro

doi:10.1006/abbi.1998.0583

Cited by 33 publications

(41 citation statements)

References 29 publications

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“…There are two enzymes encoded in the yeast genome, a mitochondrial enzyme (OSM1) and a cytoplasmic isoform (FRDS1). In contrast to membrane bound fumarate reductase in Escherichia coli and other organisms, the isoforms found in yeast are soluble and bind the electron donors FADH2 or FMNH2 noncovalently (Enomoto et al, 1996;Muratsubaki and Enomoto, 1998). Fumarate reductase is known to be highly expressed during fermentative growth.…”

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confidence: 99%

Metabolic Pathway Relationships Revealed by an Integrative Analysis of the Transcriptional and Metabolic Temperature Stress-Response Dynamics in Yeast

Walther

Strassburg

Kopka

2010

OMICS: A Journal of Integrative Biology

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The integrated analysis of omics datasets covering different levels of molecular organization has become a central task of systems biology. We investigated the transcriptional and metabolic response of yeast exposed to increased (378C) and lowered (108C) temperatures relative to optimal reference conditions (288C) in the context of known metabolic pathways. Pairwise metabolite correlation levels were found to carry more pathway-related information and to extend to farther distances within the metabolic pathway network than associated transcript level correlations. Metabolites were detected to correlate stronger to their cognate transcripts (metabolite is reactant of the enzyme encoded by the transcript) than to more remote or randomly chosen transcripts reflecting their close metabolic relationship. We observed a pronounced temporal hierarchy between metabolic and transcriptional molecular responses under heat and cold stress. Changes of metabolites were most significantly correlated to transcripts encoding metabolic enzymes, when metabolites were considered leading in time-lagged correlation analyses. By applying the concept of Granger causality, we detected directed relationships between metabolites and their cognate transcripts. When interpreted as substrate-to-product directions, most of these directed Granger causality pairs agreed with the KEGG-annotated preferred reaction direction. Thus, the introduced Granger causality approach may prove useful for determining the preferred direction of metabolic reactions in cellular systems. The metabolites glutamic acid and serine were identified as central causative metabolites influencing transcript levels at later time points. Selected examples are presented illustrating the intertwined relationships between metabolites and transcripts in the yeast temperature stress adaptation process.

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confidence: 99%

Metabolic Pathway Relationships Revealed by an Integrative Analysis of the Transcriptional and Metabolic Temperature Stress-Response Dynamics in Yeast

Walther

Strassburg

Kopka

2010

OMICS: A Journal of Integrative Biology

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“…S. cerevisiae, strain DURA (MATa his3-v leu2-3 leu2-112 trp1-289a URA3), which was obtained by integrating the URA3 gene into strain DBY747 [8], was used for the growth experiments. E. coli plasmid vector pHSG398 [9] was purchased from Takara Shuzo Co. Plasmids pFRDS and pOSM1, bearing the FRDS and OSM1 genes, respectively, were constructed during previous studies [5,6]. Two plasmids, pURAKm, which contained the URA3 gene and the kanamycin resistant (Km r ) gene from pNH-Kan/oriT plasmid [10], and pHTHAKm, which contained Lthienyl alanine resistant (THA r ) [11] gene and the Km r gene, were constructed and used for construction of the disruption cassettes of the FRDS and OSM1 genes (see Fig.…”

Section: Strains and Plasmidsmentioning

confidence: 99%

“…Yeasts contain two fumarate reductase isoenzymes that can be fractionated into the absorbed (FRDS1; fumarate reductase soluble 1) and non-absorbed (FRDS2; fumarate reductase soluble 2) fractions on a DE-52 column [4]. Recently, we determined that FRDS1, located in the cytosol, is encoded by the FRDS gene [5] and FRDS2, located in promitochondria, is encoded by the OSM1 gene [6]. Deletion of the OSM1 gene has been reported to increase the sensitivity of the yeasts to hypertonic stress [7].…”

Section: Introductionmentioning

confidence: 99%

Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth

Arikawa

1998

FEMS Microbiology Letters

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In Saccharomyces cerevisiae, the cytosolic and promitochondrial isoenzymes of fumarate reductase are encoded by the FRDS and OSM1 genes, respectively. The product of the OSM1 gene is reported to be required for growth in hypertonic medium. Simultaneous disruption of the FRDS and OSM1 genes resulted in the inability of the yeasts to grow anaerobically on glucose as a carbon source, and disruption of the OSM1 gene caused poor growth under anaerobic conditions. However, the disruption of both the FRDS and/or OSM1 genes had no effect on aerobic growth or growth under hypertonic conditions. These results suggest that the fumarate reductase isoenzymes in Saccharomyces cerevisiae are essential for anaerobic growth but not for growth under hypertonic conditions. z

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“…In the A subunit of membrane-bound FRDs and SDHs, a histidine residue (His44 in E. coli FrdA), which is the binding residue of covalently bound FAD, is highly conserved (6,37). It is also conserved in H. thermophilus FrdA, although it is not conserved in other soluble FRDs ( Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The second group of FRDs consists of soluble monomeric FRDs, and they possess the conserved catalytic region of FrdA of membrane-bound FRDs (12,37,40). Compared with the first group, few organisms are known to possess this type of FRD; these include the FRDs of several Shewanella species, Saccharomyces cerevisiae, and Trypanosoma brucei.…”

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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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One of the Fumarate Reductase Isoenzymes fromSaccharomyces cerevisiaeIs Encoded by theOSM1Gene

Cited by 33 publications

References 29 publications

Metabolic Pathway Relationships Revealed by an Integrative Analysis of the Transcriptional and Metabolic Temperature Stress-Response Dynamics in Yeast

Metabolic Pathway Relationships Revealed by an Integrative Analysis of the Transcriptional and Metabolic Temperature Stress-Response Dynamics in Yeast

Soluble fumarate reductase isoenzymes from Saccharomyces cerevisiae are required for anaerobic growth

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

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