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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

REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae.

TL;DR: Evidence is presented that REG1, a protein required for glucose repression, is a regulatory subunit of PP1 that targets its activity to proteins in the glucose repression regulatory pathway and genetic evidence indicates that the two proteins function together in regulating glucose repression.
Journal ArticleDOI

Yeast HAP2 and HAP3 activators both bind to the CYC1 upstream activation site, UAS2, in an interdependent manner.

TL;DR: In this paper, the authors show that both HAP2 and HAP3 in yeast extracts bind to UAS2UP1 and give rise to a single protein-DNA complex, termed C, in nondenaturing polyacrylamide gels.
Journal ArticleDOI

Genetics of alcohol dehydrogenase in Saccharomyces cerevisiae: I. Isolation and genetic analysis of adh mutants

TL;DR: Genetic analysis showed that two genes control synthesis of the glucose repressible enzyme ADHII, one gene the constitutive ADHI and a fourth nuclear gene the mitochondrial ADH showed any linkage.
Journal ArticleDOI

Grr1 of Saccharomyces cerevisiae is connected to the ubiquitin proteolysis machinery through Skp1: coupling glucose sensing to gene expression and the cell cycle

TL;DR: It is discovered that Grr1 physically interacts with Skp1, a protein that has been implicated in a ubiquitin‐conjugating enzyme complex that targets for degradation the cell cycle regulators Cln1 and Cln2, and the cyclin‐dependent kinase inhibitor Sic1.
Journal ArticleDOI

Glucose repression in Saccharomyces cerevisiae is directly associated with hexose phosphorylation by hexokinases PI and PII.

TL;DR: It is demonstrated that catalytically active hexokinases are indispensable for glucose repression, and the hypothesis that a specific regulatory domain of hexokinase PII exists which is independent of the hexokin enzyme PII catalytic domain is not supported.
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