Citrate synthase encoded by the CIT2 gene of Saccharomyces cerevisiae is peroxisomal.

Lewin, Alfred S.; Hines, Victoria; Small, Gillian M.

doi:10.1128/mcb.10.4.1399

Cited by 117 publications

(93 citation statements)

References 32 publications

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“…Our estimates are that in wild-type cells, the CIT1 transcript is at least 5-times more abundant than the CIT3 transcript. A CIT1 CIT2 double deletion has less than 5% the wild-type level of citrate synthase activity , and the mitochondrial fraction of a CIT1-deleted strain only has a low level of citrate synthase activity, which was originally attributed to contaminating peroxisomes (Lewin et al, 1990). Thus, under normal conditions, cit3p makes a very small contribution to the overall level of citrate synthase in the cell.…”

Section: Discussionmentioning

confidence: 99%

“…The second, cit2p, encoded by the gene CIT2, was originally shown to be extramitochondrial Rosenkrantz et al, 1986). Later, Lewin et al (1990) demonstrated that cit2p is located in the peroxisome and participates in the glyoxylate cycle. The simultaneous disruption of both CIT1 and CIT2 gives rise to a glutamate auxotrophy, which is a classical citrate synthase-deficient phenotype .…”

Section: Introductionmentioning

confidence: 99%

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The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase

Jia

Bécam

Herbert

1997

Molecular Microbiology

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase

Jia

Bécam

Herbert

1997

Molecular Microbiology

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“…While the mitochondrial Cit1 (Suissa et al, 1984) is involved in the TCA cycle, its peroxisomal isoform Cit2 functions in the glyoxylate cycle (Lewin et al, 1990). Cit3 has been identified as a mitochondrial dual-specific citrate and methylcitrate synthase functional for propionate metabolism (Graybill et al, 2007).…”

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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“…S3A). CIT2 encodes the peroxisomal citrate synthase that catalyzes the condensation of acetyl CoA and oxaloacetate to form citrate (28). Reduced growth of the isogenic Cit2:Cit2 strain in response to each compound was verified to be dependent on MTX selection (Fig.…”

Section: Specific Depletion Of the Cit2:cit2 Complex By Multiple Chemmentioning

confidence: 99%

Multiplex assay for condition-dependent changes in protein–protein interactions

Schlecht

Miranda

Suresh

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Changes in protein-protein interactions that occur in response to environmental cues are difficult to uncover and have been poorly characterized to date. Here we describe a yeast-based assay that allows many binary protein interactions to be assessed in parallel and under various conditions. This method combines molecular barcoding and tag array technology with the murine dihydrofolate reductase-based protein-fragment complementation assay. A total of 238 protein-fragment complementation assay strains, each representing a unique binary protein complex, were tagged with molecular barcodes, pooled, and then interrogated against a panel of 80 diverse small molecules. Our method successfully identified specific disruption of the Hom3:Fpr1 interaction by the immunosuppressant FK506, illustrating the assay's capacity to identify chemical inhibitors of protein-protein interactions. Among the additional findings was specific cellular depletion of the Dst1:Rbp9 complex by the anthracycline drug doxorubicin, but not by the related drug idarubicin. The assay also revealed chemical-induced accumulation of several binary multidrug transporter complexes that largely paralleled increases in transcript levels. Further assessment of two such interactions (Tpo1: Pdr5 and Snq2:Pdr5) in the presence of 1,246 unique chemical compounds revealed a positive correlation between drug lipophilicity and the drug response in yeast.protein network | cell-based assay | drug screening | chemogenomics P rotein-protein interactions (PPIs) are of fundamental importance to virtually all cellular processes, including signal transduction and regulation of gene expression. Emergent highthroughput technologies that identify protein complexes and/or binary interactions have produced a wealth of information and have further underscored the ubiquitous role that PPIs play in cell biology (1-8). Although changes in protein complexes can occur from routine biochemical signaling events (i.e., posttranslational modification, protein degradation, or relocalization), the aforementioned studies were performed under standard growth conditions, and thus network connectivity changes that occur in response to different environmental cues remain ill-defined. Measuring such changes-for example, in response to chemical (i.e., small molecule) perturbations-is valuable in understanding both cellular systems and the biological effects of the chemical in question (9).The cell's "interactome" also represents a tremendous opportunity for unique therapeutic strategies. Small-molecule drugs that directly inhibit specific PPIs could be used to modulate the activity of certain cellular processes while minimally interfering with others. PPIs are perceived to be among the most challenging targets for small molecules because of the sheer size of the interaction interface and the lack of small, deep cavities amenable to small-molecule binding (reviewed in ref. 10). Thus, despite an ever-increasing commitment by drug developers to pursue PPIs, and a growing list of small molecules th...

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Citrate synthase encoded by the CIT2 gene of Saccharomyces cerevisiae is peroxisomal.

Cited by 117 publications

References 32 publications

The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase

The CIT3 gene of Saccharomyces cerevisiae encodes a second mitochondrial isoform of citrate synthase

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

Multiplex assay for condition-dependent changes in protein–protein interactions

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