Disease relevance of CTT1

• Comparing a mutant possessing a specific lesion in CTT1 with its parental strain, it was observed that both control and ctt1 strains exhibited increased levels of lipid peroxidation after dehydration, suggesting that catalase does not protect membranes during drying [1].

High impact information on CTT1

• Consistent with a role of STREs in the induction of stress resistance, a number of other stress protein genes (e.g. HSP104) are regulated like CTT1 [2].
• The HOG pathway controls osmotic regulation of transcription via the stress response element (STRE) of the Saccharomyces cerevisiae CTT1 gene [2].
• Second, MAC1 is involved in the H2O2-induced transcription of CTT1, encoding the cytosolic catalase [3].
• This study shows that a CTT1 upstream region previously found to be involved in nitrogen, cAMP and heat control (base pairs -382 to -325) contains a UAS element (STRE, -368 to -356), which is sufficient for the activation of a reporter gene by all types of stress acting on CTT1 [4].
• As demonstrated by a gel retardation assay, the HAP1 protein binds to a heme control region of the CTT1 gene [5].

Biological context of CTT1

• Glycogen synthase (GSY2) and cytosolic catalase (CTT1) mRNA levels increase about 10-fold in wild-type cells, but this increase is not observed in ctk1Delta cells suggesting that increased message levels may require Ser(2) phosphorylation [6].
• Studies with strains with mutations in the RAS-cAMP pathway and supplementation of a rca1 mutant with cAMP show that CTT1 expression is under negative control by a cAMP-dependent protein kinase and that nutrient control of CTT1 gene expression is mediated by this pathway [7].
• Addition of oxidants of NADH was found to decrease the expression of CTT1 induced by myxothiazol treatment, suggesting that the accumulation of NADH caused by the inhibition of the respiratory chain may be involved in the signaling pathway from the mitochondria to the transcription factor [8].
• Nucleotide sequence of the Saccharomyces cerevisiae CTT1 gene and deduced amino-acid sequence of yeast catalase T [9].
• Catalase A-deficient mutants were obtained by UV mutagenesis of a ctt1 mutant strain specifically lacking catalase T [10].

Associations of CTT1 with chemical compounds

• Like the CTT1 gene, this gene is controlled by heme, oxygen and glucose [11].
• Recombinant Hansenula polymorpha as a biocatalyst: coexpression of the spinach glycolate oxidase (GO) and the S. cerevisiae catalase T (CTT1) gene [12].
• The RNAs were translated in the cell-free protein synthesis system from wheat germ, and the catalase T synthesized was isolated by immunoadsorption and polyacrylamide gel electrophoresis in the presence of dodecyl sulfate [13].
• Yeast lacking copper-zinc superoxide dismutase (CuZnSOD), manganese superoxide dismutase (SOD), catalase T, or metallothionein were studied using long-term stationary phase (10-45 days) as a simple model system to study the roles of antioxidant enzymes in aging [14].
• When cells are grown in the presence of Tween 80 the amount of catalase A, but not of catalase T, increases 4-fold [15].

Regulatory relationships of CTT1

• In contrast, Hot1p has little influence on the osmotic stress induction of CTT1, where Msn1p appears to play a more prominent role [16].
• Heat shock factor-independent heat control of transcription of the CTT1 gene encoding the cytosolic catalase T of Saccharomyces cerevisiae [17].

Other interactions of CTT1

• Expression of a CTT1-lacZ fusion in a hap1 mutant showed that the CTT1 promoter is under HAP1 control [5].
• Copper was found to specifically induce transcription of CTT1, but not CTA1, mRNA [18].
• Repression of CTT1 and SSA3 under the same conditions was also largely dependent on the presence of the sugar and also in these cases there was a strong effect when the sugar could not be phosphorylated [19].
• Re-addition of nitrogen to cells starved for nitrogen in the presence of glucose failed to trigger activation of trehalase, caused strongly reduced and aberrant repression of CTT1 and SSA3, and failed to induce the upshift in RPL25 expression [20].
• The effect of delta-aminolevulinate on catalase T-messenger RNA levels in delta-aminolevulinate synthase-defective mutants of Saccharomyces cerevisiae [13].

Analytical, diagnostic and therapeutic context of CTT1

• In a previous paper (Krawiec, Z., Biliński, T., Schüller, C. & Ruis, H., 2000, Acta Biochim. Polon. 47, 201-207) we have shown that catalase T holoenzyme is synthesized in the absence of oxygen after treatment of anaerobic yeast cultures with 0.3 M [21].

References