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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

Physiological role of glucose-phosphorylating enzymes in Saccharomyces cerevisiae

TL;DR: Starting with a mutant of Saccharomyces cerevisiae lacking glucokinase and both the hexokinase isozymes P1 and P2, strains were constructed, by genetic crosses, that carry single glucose-phosphorylating enzymes.
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Structure and molecular analysis of RGR1, a gene required for glucose repression of Saccharomyces cerevisiae.

TL;DR: The cloned RGR1 gene suppressed all of the phenotypes caused by the mutation and encoded a 3.6-kilobase poly(A)+ RNA, and rgr1 was shown to be a new locus, which was predicted to encode a 123-kilodalton protein.
Journal ArticleDOI

Analysis of the galactose signal transduction pathway in Saccharomyces cerevisiae: interaction between Gal3p and Gal80p.

TL;DR: It is demonstrated that concomitant overproduction of the negative regulator, Gal80p, and Gal3p suppresses this constitutive GAL expression, and formation of theGal80p-Gal3p complex depends on the normal function of Gal3P.
Journal ArticleDOI

Purification and molecular cloning of the "A" chain of a rat heteromeric CCAAT-binding protein. Sequence identity with the yeast HAP3 transcription factor.

TL;DR: The deduced amino acid sequence of the A chain showed a remarkable identity over a length of 90-amino acid residues with a sequences of the Hap3 polypeptide, a component of a heteromeric multisubunit yeast transcription factor.
Journal ArticleDOI

Control of mRNA turnover as a mechanism of glucose repression in Saccharomyces cerevisiae.

TL;DR: A working hypothesis with the following major features is proposed: the carbon source, via a signaling pathway involving kinase/phosphatase activities, controls the rate of initiation, and thus influences a competition between eukaryotic initiation factors binding to the capped mRNA and a decapping activity which is one of the rate limiting activities in the turnover of such mRNAs.
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