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Yeast Carbon Catabolite Repression

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TLDR
It is possible in certain cases to propose a partial model of the way in which the different elements involved in catabolite repression may be integrated, and preliminary evidence suggests that Snf1 is in a dephosphorylated state under these conditions.
Abstract
Glucose and related sugars repress the transcription of genes encoding enzymes required for the utilization of alternative carbon sources; some of these genes are also repressed by other sugars such as galactose, and the process is known as catabolite repression. The different sugars produce signals which modify the conformation of certain proteins that, in turn, directly or through a regulatory cascade affect the expression of the genes subject to catabolite repression. These genes are not all controlled by a single set of regulatory proteins, but there are different circuits of repression for different groups of genes. However, the protein kinase Snf1/Cat1 is shared by the various circuits and is therefore a central element in the regulatory process. Snf1 is not operative in the presence of glucose, and preliminary evidence suggests that Snf1 is in a dephosphorylated state under these conditions. However, the enzymes that phosphorylate and dephosphorylate Snf1 have not been identified, and it is not known how the presence of glucose may affect their activity. What has been established is that Snf1 remains active in mutants lacking either the proteins Grr1/Cat80 or Hxk2 or the Glc7 complex, which functions as a protein phosphatase. One of the main roles of Snf1 is to relieve repression by the Mig1 complex, but it is also required for the operation of transcription factors such as Adr1 and possibly other factors that are still unidentified. Although our knowledge of catabolite repression is still very incomplete, it is possible in certain cases to propose a partial model of the way in which the different elements involved in catabolite repression may be integrated.

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References
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Journal ArticleDOI

GAL4 of Saccharomyces cerevisiae activates the lactose-galactose regulon of Kluyveromyces lactis and creates a new phenotype: glucose repression of the regulon.

TL;DR: Results indicate that the GAL4 and LAC9 proteins activate transcription in a similar manner, however, either the LAC8 or GAL5 gene or a product of these genes responds differently to glucose in K. lactis.
Journal ArticleDOI

Functional analysis of histones H2A and H2B in transcriptional repression in Saccharomyces cerevisiae.

TL;DR: Results suggest that repressive chromatin structure may be established through the interactions of the Spt proteins with these histones, and other proteins, the products of the HIR (histone regulation) genes, may function to direct H2A and H2B to specific promoters.
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ACR1, a gene encoding a protein related to mitochondrial carriers, is essential for acetyl-CoA synthetase activity in Saccharomyces cerevisiae.

TL;DR: Genetic and biochemical characterization show that, in this mutant, the structural gene for acetyl-CoA synthetase is not affected and the ACR1 gene product is an integral membrane protein related to the family of mitochondrial carriers.
Journal ArticleDOI

Cyclic amp-dependent protein kinase inhibits adh2 expression in part by decreasing expression of the transcription factor gene adr1

TL;DR: It is demonstrated that the decreased abundance of Adr1p in bcy1 mutant cells contributes to the inhibition of ADH2 expression, and some of these mechanisms may impinge upon events at or subsequent to the ADR1-dependent step in ADH 2 transcriptional activation.
Journal ArticleDOI

ADR1c mutations enhance the ability of ADR1 to activate transcription by a mechanism that is independent of effects on cyclic AMP-dependent protein kinase phosphorylation of Ser-230

TL;DR: It is suggested thatADR1c mutations enhance ADR1 activity by blocking cAPK phosphorylation and inactivation of Ser-230, and may block the binding of a repressor to ADr1 or alter the structure of ADR 1 so that transcriptional activation regions become unmasked.
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