scispace - formally typeset
Open AccessJournal ArticleDOI

Yeast Carbon Catabolite Repression

Reads0
Chats0
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.

read more

Content maybe subject to copyright    Report

Citations
More filters
Journal ArticleDOI

The hexokinase 2 protein regulates the expression of the GLK1, HXK1 and HXK2 genes of Saccharomyces cerevisiae.

TL;DR: Findings reveal a novel mechanism of gene regulation whereby the product of a glycolytic gene, normally resident in the cytosol, interacts directly with nuclear proteins to regulate the transcription of the HXK1 and GLK1 genes and to autoregulate its own transcription.
Journal ArticleDOI

Regulation of methanol utilisation pathway genes in yeasts

TL;DR: In this paper, the role of cis and trans acting factors in the expression of methanol utilisation pathway genes is reviewed both in the context of the native cell environment as well as in heterologous hosts.
Journal ArticleDOI

Glucose and Sucrose Act as Agonist and Mannose as Antagonist Ligands of the G Protein-Coupled Receptor Gpr1 in the Yeast Saccharomyces cerevisiae

TL;DR: The results obtained by cysteine scanning mutagenesis and SCAM of residues in TMD VI provide strong evidence that glucose and sucrose directly interact as ligands with Gpr1 and that the ligand repertoire of GPCRs can be extended to common sugars in millimolar concentrations.
Journal ArticleDOI

Integration of gene expression data into genome-scale metabolic models.

TL;DR: A framework for integration of transcriptome data into stoichiometric metabolic models to obtain improved flux predictions is presented, to exploit the regulatory information in the expression data to give additional constraints on the metabolic fluxes in the model.
Journal ArticleDOI

Transcript profiling in Candida albicans reveals new cellular functions for the transcriptional repressors CaTup1, CaMig1 and CaNrg1.

TL;DR: The targets of CaMig1 and CaNrg1 repression, and phenotypic analyses of nrg1/nrg1 and mig1/mig1 mutants, indicate that these factors play differential roles in the regulation of metabolism, cellular morphogenesis and stress responses.
References
More filters
Journal ArticleDOI

Exploring the Metabolic and Genetic Control of Gene Expression on a Genomic Scale

TL;DR: DNA microarrays containing virtually every gene of Saccharomyces cerevisiae were used to carry out a comprehensive investigation of the temporal program of gene expression accompanying the metabolic shift from fermentation to respiration, and the expression patterns of many previously uncharacterized genes provided clues to their possible functions.
Journal ArticleDOI

A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A

TL;DR: A new cellular p300/CBP-associated factor (P/CAF) having intrinsic histone acetylase activity has been identified that competes with E1A, a new adenoviral oncoprotein that induces progression through the cell cycle by binding to the products of the p300 and retinoblastoma gene families.
Journal ArticleDOI

The AMP‐Activated Protein Kinase

TL;DR: The central hypothesis is that the AMP-activated protein kinase cascade appears to be an ancient system which evolved to protect cells against the effects of nutritional or environmental stress, and protects the cell by switching off ATP-consuming pathways and switching on alternative pathways for ATP generation.
Journal ArticleDOI

Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase

TL;DR: A model is proposed to account for the synthesis and regulation of the two forms of inverts: the larger, regulated mRNA contains the initiation codon for the signal sequence required for synthesis of the secreted, glycosylated form of invertase; the smaller, constitutively transcribed mRNA begins within the coding region of the signal sequences, resulting in synthesis ofThe intracellular enzyme.
Journal ArticleDOI

Characterization of the AMP-activated Protein Kinase Kinase from Rat Liver and Identification of Threonine 172 as the Major Site at Which It Phosphorylates AMP-activated Protein Kinase

TL;DR: This finding is consistent with the recent report that the AMP-activated protein kinase kinase can slowly phosphorylate and activate calmodulin-dependentprotein kinase I, at least in vitro.
Related Papers (5)