Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism of<i>S.cerevisiae</i>

Hartig, Andreas; Simon, Manuel; Schuster, Tillman; Daugherty, Jon R.; Yoo, Hyang Sook; Cooper, Terrance G.

doi:10.1093/nar/20.21.5677

Cited by 92 publications

(86 citation statements)

References 41 publications

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“…Only a weak band was detected in the preparation from glycerol. A similar regulation was reported for the transcription of the gene encoding the malatc synthase isoenzyme functioning in the glyoxylate pathway [17,18].…”

Section: Regulation Of Icll Gene Expressionsupporting

confidence: 75%

Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae

Fernández

Moreno

et al. 1993

FEBS Letters

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In this work, we studied the transcriptional regulation of isocitrate lyase synthesis. In Northern blot analyses we first showed that the steady-state ICLl mRNA levels depend on the carbon source used for growth. In addition, we determined the kinetics of transcriptional repression upon a shift of ethanol-grown cells to glucose and of the induction when cells were transferred from glucose to ethanol. By deletion analyses as well as by studying the influence on expression of different fragments cloned into the heterologous CYCZ promoter lacking its own UAS sequences, we defined UAS and URS elements in the ICLI promoter. A region mediating the control by CAT3, a gene also involved in the control of expression of other genes subject to carbon catabolite repression, was found to overlap with one of these CJAS elements.

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Section: Regulation Of Icll Gene Expressionsupporting

confidence: 75%

Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae

Fernández

Moreno

et al. 1993

FEBS Letters

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“…It thus appears that the succinate dehydrogenase complex (SDHC), a tetramer of Sdh1, Sdh2, Sdh3 and Sdh4 (Lombardo et al, 1990;Chapman et al, 1992;Bullis and Lemire, 1994;Daignan-Fornier et al, 1994), is the only TCA cycle-specific enzyme required for acetate utilization on YNBA. Our results also show that the enzymes involved in the glyoxylate cycle operation, such as ACO (Aco1) (Gangloff et al, 1990), malate synthase (Mls1) (Hartig et al, 1992;Kunze et al, 2002), isocitrate lyase (Icl1) (Fernandez et al, 1992;Taylor et al, 1996) and Mdh2 (Minard and McAlister-Henn, 1991), are indispensable for the growth of yeast cells with acetate on YNBA, regardless of their involvement in the TCA cycle. Considering that both the cytoplasmic and mitochondrial isoforms of fumarase (FUM) are encoded by a single gene, FUM1 (Wu and Tzagoloff, 1987), and that operation of the TCA cycle is dispensable on YNBA, as shown above, it is suggested that conversion of fumarate to malate Figure 6.…”

Section: Succinate-fumarate Carrier (Sfc1) Is Essential For Acetate Usupporting

confidence: 54%

“…The first two enzymes, ICL and MLS, are unique to the glyoxylate cycle and are encoded by ICL1 (Fernandez et al, 1992;Taylor et al, 1996) and MLS1 (Hartig et al, 1992;Kunze et al, 2002), respectively. Icl1 is localized solely in the cytosol, even under growth conditions that induce peroxisome proliferation, and its presence in peroxisomes is not essential for a functional glyoxylate cycle (Taylor et al,154 Y. J.…”

Section: Introductionmentioning

confidence: 99%

TCA cycle‐independent acetate metabolism via the glyoxylate cycle in Saccharomyces cerevisiae

Lee

Jang

Kim

et al. 2010

Yeast

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In Saccharomyces cerevisiae, the accepted theory is that due to TCA cycle dysfunction, the cit1 mutant lacking the mitochondrial enzyme citrate synthase (Cit1) cannot grow on acetate, regardless of the presence of the peroxisomal isoenzyme (Cit2). In this study, we re-evaluated the roles of Cit1 and Cit2 in acetate utilization and examined the pathway of acetate metabolism by analysing mutants defective in TCA or glyoxylate cycle enzymes. Although cit1 cells showed significantly reduced growth on rich acetate medium (YPA), they exhibited growth similar to cit2 and the wild-type cells on minimal acetate medium (YNBA). Impaired acetate utilization by cit1 cit2 cells on YNBA was restored by ectopic expression of either Cit2 or its cytoplasmically localized variants. Deletion of any of the genes for the enzymes solely involved in the TCA cycle (IDH1, KGD1 and LSC1 ), except for SDH1, caused little defect in acetate utilization on YNBA but resulted in significant growth impairment on YPA. In contrast, cells lacking any of the genes involved in the glyoxylate cycle (ACO1, FUM1, MLS1, ICL1 and MDH2 ) did not grow on either YNBA or YPA. Deletion of SFC1 encoding the succinate-fumarate carrier also caused similar growth defects on YNBA. Our results suggest that in S. cerevisiae the glyoxylate cycle functions as a competent metabolic pathway for acetate utilization on YNBA, while both the TCA and glyoxylate cycles are essential for growth on YPA.

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“…A larger malate synthase may also be found in Succhuromyces cerevisiae according to a transcript revealed under certain specific conditions [25]. Several observations exclude the possibility that the assignment of the larger size for MSG was due to an artifact or sequencing error: (a) the enzyme protein purified from wild-type cells displayed a molecular mass in accordance with that calculated from the corresponding deduced amino acid sequence; (b) the peptide sequence of the N-terminal fragment indicates that the ATG initiation codon is correctly assigned.…”

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of Escherichia coli Malate Synthase G

Molina

Pellicer

Badı́a

et al. 1994

European Journal of Biochemistry

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Two genes encoding the enzymes malate synthase G and glycolate oxidase, have been linked to locus glc (64.5 min), responsible for glycolate utilization in Escherichia coli. The gene encoding malate synthase G, for which we propose the notation glcB, has been cloned, sequenced and found to correspond to a 2262-nucleotide open-reading frame, which can encode a 723-amino-acid polypeptide, clearly different from the isoenzyme malate synthase A, which has 533 amino acids. Northern-blot experiments indicate that glcB was expressed as an apparently monocistronic transcript, inducible by glycolate. Malate synthase G was purified to near homogeneity. The molecular mass determined by gel filtration yielded a value of 82 kDa for the purified enzyme and the same value as for the crude extract enzyme, indicating a monomeric structure. Despite the lower sequence similarity between malate synthase G and the other reported malate synthases, three out of nine consensus boxes defined in most of these enzymes are conserved in addition to a cysteine residue that has been reported to be important for the catalytic mechanisms.Two isoenzymes of malate synthase have been described for the metabolism of glyoxylate in Escherichia coli. Malate synthase A (MSA), involved in the glyoxylate by-pass reaction, is encoded by the gene aceB belonging to the ace operon located at 91 min on the genetic map [l], and is predominant (60% total activity) in cells metabolizing the glyoxylate formed in the dissimilation of acetate [2]. The other isoenzyme, malate synthase G (MSG), encoded by a gene mapped in the locus glc, accounts for almost the entire malate-synthesizing activity in cells metabolizing the glyoxylate formed during growth on glycolate [2]. Both isoenzymes catalyze the condensation of glyoxylate and acetyl-CoA to yield malate, display very similar kinetic parameters for the substrate (31, and are distinguished on the basis of their chromatographic separation, thermostability and sensitivity to inhibitors such as glycolate and oxalate [3].In glycolate metabolism, this compound is first oxidized to glyoxylate by the action of glycolate oxidase [4, 51. Glyoxylate is subsequently metabolized by two divergent codensation reactions; one reaction is catalyzed by glyoxylate carboligase, which converts two glyoxylate molecules to tartronic semialdehyde and carbon dioxide [6], and the other reaction is catalyzed by MSG. The latter process can be considered a reaction of an oxidative pathway if glyoxylate is metabolized through the dicarboxylic cycle, or a reaction of Correspondence to L. Baldomi,

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Differentially regulated malate synthase genes participate in carbon and nitrogen metabolism ofS.cerevisiae

Cited by 92 publications

References 41 publications

Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae

Transcriptional regulation of the isocitrate lyase encoding gene in Saccharomyces cerevisiae

TCA cycle‐independent acetate metabolism via the glyoxylate cycle in Saccharomyces cerevisiae

Molecular Characterization of Escherichia coli Malate Synthase G

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