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PubMed1975

Kinetics of induced and repressed enzyme synthesis in Saccharomyces cerevisiae.

Our previous work has shown that both induction, after addition of inducer, and loss of ability to produce allophanate hydrolase, after removal of inducer, proceed more rapidly than expected from the reported half-life of messenger ribonucleic acid in Saccharomyces cerevisiae. As a basis of rectifying these observations, we have characterized induction and repression of allophanate hydrolase synthesis and find that: (i) induction of the hydrolase begins immediately upon addition of inducer, (ii) once induction has been initiated removal of inducer does not result in immediate loss of synthetic capacity, (iii) induction of the capacity to produce hydrolase can occur in the absence of protein synthesis, (iv) the half-life of hydrolase synthetic capacity increases if protein synthesis is inhibited, (v) allophanate hydrolase itself is not degraded upon removal of inducer, and (vi) induction and repression of allophanate hydrolase synthetic capacity likely occurs at the level of transcription.

Amidohydrolases↗
PubMed1969

Role of isoleucyl-transfer ribonucleic acid synthetase in ribonucleic acid synthesis and enzyme repression in yeast.

Temperature-sensitive mutations in the isoleucyl-transfer ribonucleic acid (tRNA) synthetase of yeast, ilS(-)1-1 and ilS(-)1-2, were used to examine the role of aminoacyl-tRNA synthetase enzymes in the regulation of ribonucleic acid (RNA) synthesis and enzyme synthesis in a eucaryotic organism. At the permissive temperature, 70 to 100% of the intracellular isoleucyl-tRNA was charged in mutants carrying these mutations; at growth-limiting temperatures, less than 10% was charged with isoleucine. Other aminoacyl-tRNA molecules remained essentially fully charged under both conditions. Net protein and RNA syntheses were rapidly inhibited when the mutant was shifted from the permissive to the restrictive temperature. Most of the ribosomes remained in polyribosome structures at the restrictive temperature even though protein synthesis was strongly inhibited. Two of the enzymes of isoleucine biosynthesis, threonine deaminase and acetohydroxyacid synthetase, were derepressed about twofold during slow growth of the mutants at a growth-limiting temperature. This is about the same degree of derepression that is achieved by growth of an auxotroph on limiting isoleucine. We conclude that charged aminoacyl-tRNA is essential for RNA synthesis and for the multivalent repression of the isoleucine biosynthetic enzymes. Aminoacyl tRNA synthetase enzymes appear to play important regulatory roles in the cell physiology of eucaryotic organisms.

Enzyme Repression↗
PubMed1981

Effect of unsaturated fatty acids on the biosynthesis of glucose-repressed enzymes in yeast.

In anaerobically glucose-grown yeast isocitrate lyase (EC 4.1.3.1.), and malate dehydrogenase (EC 1.1.1.37.) are repressed by glucose. 24 h cultures still contain 0.3--0.4% glucose in the medium, which is enough to completely repress these activities. Aeration of these cells, in buffer containing acetate, initiates the formation of the three enzymes. Within 16 h, the specific activities of these enzymes increase about 140, 120 and 70-fold, respectively. Glucose-6-phosphate dehydrogenase activity was not altered. When the yeast was grown anaerobically, but with a supplement of an unsaturated fatty acid in the medium, synthesis of the three enzymes was much faster and the specific activities after 16 h of derepression were considerably higher. A relationship exists between the number of double bonds in the unsaturated fatty acid molecule and its capability to stimulate enzyme synthesis: linolenic acid is more effective than linoleic acid, which, in turn, is much more effective than oleic acid. Increasing periods of aeration with glucose of anaerobically grown cells prior to derepression results in an increasing stimulation of enzyme synthesis on subsequent derepression. Anaerobic incubation of yeast in the presence of an unsaturated fatty acid in advance to derepression also increased the velocity of enzyme formation. It is suggested that during the aeration period with glucose and during anaerobic incubation with an unsaturated fatty acid a more active protein synthesizing apparatus was formed.

Fatty Acids, Unsaturated↗
PubMed1980

Enhancement of toxicity and enzyme-repressing activity of p-dioxane by chlorination: stereoselective effects.

The acute toxicity of p-dioxane may be enhanced up to 1000-fold by chlorination of the compound. The effect was stereoselective. Of the stereoisomers tested, tetrachloro-p-dioxane, isomer I (2r, 3t, 5t, 6c) was over 80 times more toxic than isomer II (2r, 3c, 5t, 6t). The latter compound was also a potent repressor of hepatic dimethylnitrosamine-demethylase I (DMN-d) and aryl hydrocarbon hydroxylase (AHH).

Animals↗
PubMed1987

Reversal by cyclic AMP of the urea-induced inhibition of synthesis of a catabolite-repressible enzyme in Vibrio cholerae.

Low concentrations of urea, which did not inhibit the synthesis of the catabolite nonrepressible enzyme alkaline phosphatase in Vibrio cholerae, or markedly affect its overall growth, specifically inhibited the expression of the tryptophanase operon in a temperature-dependent manner. However, in contrast to what is found in Escherichia coli, this urea-induced inhibition of tryptophanase synthesis in V. cholerae could be almost completely relieved by exogenously added cyclic AMP. The possible mechanism of the process is discussed.

Alkaline Phosphatase↗