High cAMP Levels Antagonize the Reprogramming of Gene Expression that Occurs at the Diauxic Shift in Saccharomyces Cerevisiae

Boy‐Marcotte, Emmanuelle; Tadi, Djamila; Perrot, Michel; Boucherie, Hélian; Jacquet, Michel

doi:10.1099/13500872-142-3-459

Cited by 77 publications

(96 citation statements)

References 43 publications

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“…Yeast strains and media: The S. cerevisiae strains used for this work are OL556 (MATa/MATa, cdc25-5/cdc25-5 his3/his3 leu2/ leu2 trp1/TRP1 rca1/rca1 ura3/ura3) (Boy-Marcotte et al 1996), 74D694 (MATa ade1-14 trp1-289 leu2-3,112 his3-200 ura3-52) ½psiÀ; ½psi1 (Derkatch et al 1998), MT557/3b (MATa ade2-1 sup45-2 leu2-3,112 ura3-1 his5-2) (Stansfield et al 1995a), and FS1 (MATa, ade2-592 lys2-201 leu2-3,112 his3-200 ura3-52) (Namy et al 2001).…”

Section: Methodsmentioning

confidence: 99%

Fine-Tuning of Translation Termination Efficiency inSaccharomyces cerevisiaeInvolves Two Factors in Close Proximity to the Exit Tunnel of the Ribosome

et al. 2007

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In eukaryotes, release factors 1 and 3 (eRF1 and eRF3) are recruited to promote translation termination when a stop codon on the mRNA enters at the ribosomal A-site. However, their overexpression increases termination efficiency only moderately, suggesting that other factors might be involved in the termination process. To determine such unknown components, we performed a genetic screen in Saccharomyces cerevisiae that identified genes increasing termination efficiency when overexpressed. For this purpose, we constructed a dedicated reporter strain in which a leaky stop codon is inserted into the chromosomal copy of the ade2 gene. Twenty-five antisuppressor candidates were identified and characterized for their impact on readthrough. Among them, SSB1 and snR18, two factors close to the exit tunnel of the ribosome, directed the strongest antisuppression effects when overexpressed, showing that they may be involved in fine-tuning of the translation termination level.

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Section: Methodsmentioning

confidence: 99%

Fine-Tuning of Translation Termination Efficiency inSaccharomyces cerevisiaeInvolves Two Factors in Close Proximity to the Exit Tunnel of the Ribosome

et al. 2007

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“…The changes in protein synthesis during the diauxic shift were also investigated. Two-dimensional gel electrophoresis showed that many proteins are affected (6,7). These large scale analyses showed the complexity of the regulations occurring at the diauxic shift.…”

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confidence: 99%

The Transcriptional Activator Cat8p Provides a Major Contribution to the Reprogramming of Carbon Metabolism during the Diauxic Shift in Saccharomyces cerevisiae

Haurie¹,

Perrot²,

Mini³

et al. 2001

Journal of Biological Chemistry

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149

136

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In yeast, the transition between the fermentative and the oxidative metabolism, called the diauxic shift, is associated with major changes in gene expression and protein synthesis. The zinc cluster protein Cat8p is required for the derepression of nine genes under nonfermentative growth conditions (ACS1, FBP1, ICL1, IDP2, JEN1, MLS1, PCK1, SFC1, and SIP4). To investigate whether the transcriptional control mediated by Cat8p can be extended to other genes and whether this control is the main control for the changes in the synthesis of the respective proteins during the adaptation to growth on ethanol, we analyzed the transcriptome and the proteome of a cat8⌬ strain during the diauxic shift. In this report, we demonstrate that, in addition to the nine genes known as Cat8p-dependent, there are 25 other genes or open reading frames whose expression at the diauxic shift is altered in the absence of Cat8p. For all of the genes characterized here, the Cat8p-dependent control results in a parallel alteration in mRNA and protein synthesis. It appears that the biochemical functions of the proteins encoded by Cat8p-dependent genes are essentially related to the first steps of ethanol utilization, the glyoxylate cycle, and gluconeogenesis. Interestingly, no function involved in the tricarboxylic cycle and the oxidative phosphorylation seems to be controlled by Cat8p.

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“…Indeed, it has been shown that the signal that coordinately regulates carbon and nitrogen metabolism in Escherichia coli depends on the intracellular levels of ␣-ketoglutarate and glutamine (15). Interestingly, the presence of Gdh3p has been found to be increased during diauxic transition in S. cerevisiae (16), suggesting a particular role of this enzyme in respiratory metabolism.…”

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confidence: 99%

NADP-Glutamate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae

DeLuna¹,

Avendaño

Riego

et al. 2001

Journal of Biological Chemistry

140

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In the yeast Saccharomyces cerevisiae, two NADP؉ -dependent glutamate dehydrogenases (NADP-GDHs) encoded by GDH1 and GDH3 catalyze the synthesis of glutamate from ammonium and ␣-ketoglutarate. The GDH2-encoded NAD ؉ -dependent glutamate dehydrogenase degrades glutamate producing ammonium and ␣-ketoglutarate. Until very recently, it was considered that only one biosynthetic NADP-GDH was present in S. cerevisiae. This fact hindered understanding the physiological role of each isoenzyme and the mechanisms involved in ␣-ketoglutarate channeling for glutamate biosynthesis. In this study, we purified and characterized the GDH1-and GDH3-encoded NADP-GDHs; they showed different allosteric properties and rates of ␣-ketoglutarate utilization. Analysis of the relative levels of these proteins revealed that the expression of GDH1 and GDH3 is differentially regulated and depends on the nature of the carbon source. Moreover, the physiological study of mutants lacking or overexpressing GDH1 or GDH3 suggested that these genes play nonredundant physiological roles. Our results indicate that the coordinated regulation of GDH1-, GDH3-, and GDH2-encoded enzymes results in glutamate biosynthesis and balanced utilization of ␣-ketoglutarate under fermentative and respiratory conditions. The possible relevance of the duplicated NADP-GDH pathway in the adaptation to facultative metabolism is discussed.

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High cAMP Levels Antagonize the Reprogramming of Gene Expression that Occurs at the Diauxic Shift in Saccharomyces Cerevisiae

Abstract: cAMP and gene expression in S. cerevisiae yeast, Ras proteins are controlling elements of adenylate cyclase.

Cited by 77 publications

References 43 publications

Fine-Tuning of Translation Termination Efficiency inSaccharomyces cerevisiaeInvolves Two Factors in Close Proximity to the Exit Tunnel of the Ribosome

Fine-Tuning of Translation Termination Efficiency inSaccharomyces cerevisiaeInvolves Two Factors in Close Proximity to the Exit Tunnel of the Ribosome

The Transcriptional Activator Cat8p Provides a Major Contribution to the Reprogramming of Carbon Metabolism during the Diauxic Shift in Saccharomyces cerevisiae

NADP-Glutamate Dehydrogenase Isoenzymes of Saccharomyces cerevisiae

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