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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

Two zinc fingers of a yeast regulatory protein shown by genetic evidence to be essential for its function

TL;DR: Evidence is provided that the invariant cysteine and histidine residues are essential for the formation of the finger structure of the helix-turn-helix motif1, the best-understood protein structure involved in DNA binding.

TheMutantType1Protein Phosphatase Encoded byglc7-1 fromSaccharomyces cerevisiae Fails ToInteract Productively withtheGAC1-Encoded Regulatory Subunit

Abstract: Loss-of-function gac1 mutants of Saccharomyces cerevisiae fail to accumulate normal levels of glycogen because of low glycogen synthase activity. Increased dosage of GAC1 results in increased activity of glycogen synthase and a corresponding hyperaccumulation of glycogen. The glycogen accumulation phenotype of gac1 is similar to that of glc7-1, a type 1 protein phosphatase mutant. We have partially characterized the GAC1 gene product (Gac1p) and show that levels of Gac1p increase during growth with the same kinetics as glycogen accumulation. Gac1p is phosphorylated in vivo and is hyperphosphorylated in a glc7-1 mutant. Gac1p and the type 1 protein phosphatase directly interact in vitro, as assayed by coimmunoprecipitation, and in vivo, as determined by the dihybrid assay described elsewhere (S. Fields and O.-k. Song, Nature [London] 340:245-246, 1989). The interaction between Gac1p and the glc7-1-encoded form of the type 1 protein phosphatase is defective, as assayed by either immunoprecipitation or the dihybrid assay. Increased dosage of GAC1 partially suppresses the glycogen defect of glc7-1. Collectively, our data support the hypotheses that GAC1 encodes a regulatory subunit of type 1 protein phosphatase and that the glycogen accumulation defect of glc7-1 is due at least in part to the inability of the mutant phosphatase to interact with its regulatory subunit.
Journal ArticleDOI

ADA5/SPT20 links the ADA and SPT genes, which are involved in yeast transcription.

TL;DR: Most interestingly, ADA5 is identical to SPT20, showing that it shares phenotypes with the ADA and SPT family of genes, and presents a speculative pathway of transcriptional activation involving the ADA2-ADA3-GCN5-ADA5 complex and the TATA-binding protein.
Journal ArticleDOI

Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae

TL;DR: Results suggest that activation of Cdc28p kinase requires proteolysis, and a human cDNA encoding a regulatory subunit of the 26S proteasome, p31, which was found to be a homolog of Nin1p, is cloned.
Journal ArticleDOI

New genes involved in carbon catabolite repression and derepression in the yeast Saccharomyces cerevisiae.

TL;DR: It is shown that carbon metabolism in yeast cells is under a very complex and ramified control of repressing and derepressing genes, which are interdependent.
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