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PubMed1976

[Effect of detergents and proteolytic enzymes on membrane-bound phosphohydrolases in Escherichia coli cells with repressed and depressed biosynthesis of these enzymes].

Solubilization of protein membranes by detergents and protein liberation from the membranes induced by proteolytic enzymes results in a change of activity of membrane-bound phosphohydrolases--alkaline phosphatase and polyphosphatase. The activity of enzymes under conditions of repressed and derepressed biosynthesis of phosphohydrolases changes differently, thus indicating their different membrane environment in the two types of membranes. Some data were obtained on the localization of alkaline phosphatase in a hydrophobic region, possibly in lipid bilayer and polyphosphatase in the surface layers of the membrane.

Binding Sites↗
PubMed1971

Mutants of Salmonella typhimurium with an altered leucyl-transfer ribonucleic acid synthetase.

Two trifluoroleucine-resistant mutants of Salmonella typhimurium, strains CV69 and CV117, had an altered leucyl-transfer ribonucleic acid (tRNA) synthetase. The mutant enzymes had higher apparent K(m) values for leucine (ca. 10-fold) and lower specific activities (ca. twofold) than the parent enzyme when tested in crude extracts. Preparations of synthetase purified ca. 60-fold from the parent and strain CV117 differed sixfold in their leucine K(m) values. In addition, the mutant enzyme was inactivated faster than the parent enzyme at 50 C. The growth rates of strains CV69 and CV117 at 37 C were not significantly different from that of the parent, whereas at 42 C strain CV69 grew more slowly than the parent. Leucine-, valine-, and isoleucine-forming enzymes were partially derepressed when the mutants were grown in minimal medium; the addition of leucine repressed these enzymes to wild-type levels. During growth in minimal medium, the proportion of leucine tRNA that was charged in the mutants was about 75% of that in the parent. The properties of strain CV117 were shown to result from a single mutation located near gal at minute 18 on the genetic map. These studies suggest that leucyl-tRNA synthetase is involved in repression of the enzymes required for the synthesis of branched-chain amino acids.

Adenosine Triphosphate↗
PubMed1980

Glycolytic enzymes and intermediates in carbon catabolite repression mutants of Saccharomyces cerevisiae.

Glycolytic parameters were determined in recessive yeast mutants with partial defects in carbon catabolite repression. Specific activities of pyruvate kinase and pyruvate decarboxylase in glucose grown cells of all mutant and wild type strains were 4--5 times higher than in ethanol grown cells. Mutants of gene HEX1 had a reduced hexose phosphorylating activity on all media whereas those of gene HEX2 had elevated levels but only in glucose grown cells. Mutants of gene CAT80 were normal in this respect. All other glycolytic enzymes were normal in all mutants. This was also true for glycolytic intermediates. Only hex1-mutants showed a reduced fermentation of repressing sugars. The three genes appear to be involved in catabolite repression of several but not of all repressible enzymes. Even though all three types of mutants show a limited overlap in their effects on certain enzymes, they still are distinctly different in their action spectra. Carbon catabolite repression apparently does not depend on the sole accumulation of glycolytic intermediates. The activity of the products of the three genes HEX1, HEX2 and CAT80 are required directly or indirectly for triggering carbon catabolite repression. Even a small segment of carbon catabolite repression is controlled by several genes with regulatory functions indicating that the entire regulatory circuit is highly complex.

Carbon↗
PubMed2005

Regulation of the pyrimidine biosynthetic pathway in Pseudomonas mucidolens.

Control of pyrimidine biosynthesis was examined in Pseudomonas mucidolens ATCC 4685 and the five de novo pyrimidine biosynthetic enzyme activities unique to this pathway were influenced by pyrimidine supplementation in cells grown on glucose or succinate as a carbon source. When uracil was supplemented to glucose-grown ATCC 4685 cells, activities of four de novo enzymes were depressed which indicated possible repression of enzyme synthesis. To learn whether the pathway was repressible, pyrimidine limitation experiments were conducted using an orotate phosphoribosyltransferase (pyrE) mutant strain identified in this study. Compared to excess uracil growth conditions for the glucose-grown mutant strain cells, pyrimidine limitation of this strain caused aspartate transcarbamoylase, dihydroorotase and dihydroorotate dehydrogenase activities to increase by more than 3-fold while OMP decarboxylase activity increased by 2.7-fold. The syntheses of the de novo enzymes appeared to be regulated by pyrimidines. At the level of enzyme activity, aspartate transcarbamoylase activity in P. mucidolens ATCC 4685 was subject to inhibition at saturating substrate concentrations. Transcarbamoylase activity was strongly inhibited by UTP, ADP, ATP, GTP and pyrophosphate.

Aspartate Carbamoyltransferase↗
PubMed1989

A single, phosphate-repressible deoxyribonuclease, DNase A, secreted in Aspergillus nidulans.

High levels of nuclease activities were identified in filtrates of Aspergillus cultures after growth in low-but not in high-phosphate media. Deoxyribonuclease activities, characterized extensively by column chromatography, showed a coincident single peak for ss- and ds-DNase which was distinct from the peak for RNase. Both ss-DNase and ds-DNase are endonucleolytic and showed the highest activity in the presence of Ca2+ and Mn2+ (at pH 8.0). They also showed identical heat sensitivities suggesting that a single, phosphate-repressible DNase was secreted. This enzyme, therefore, corresponds to the well-characterized extracellular DNase A of Neurospora. However, the Aspergillus DNase A did not cross-react with antisera to secreted Neurospora nucleases and showed different chromatographic properties, and active peptides of different sizes were visualized on DNA activity gels. The increasing derepression of Aspergillus DNase A by decreasing phosphate levels was similar to that of secreted alkaline phosphatase and these increases were both abolished by the regulatory mutant palcA.

Aspergillus nidulans↗
PubMed1977

Design of molecular control mechanisms and the demand for gene expression.

Regulation by a repressor protein is the mechanism selected when, in the organism's natural environment, there is low demand for expression of the regulated structural genes. Regulation by an activator protein is selected when there is high demand for expression of the regulated structural genes. These general conclusions are useful in relating physiological function to underlying molecular determinants in a wide variety of systems that includes repressible biosynthetic pathways, inducible biosynthetic enzymes, inducible drug resistance, and prophage induction, as well as inducible catabolic pathways, for which a special case of this prediction previously was reported [Savageau, M. A. (1974) Proc. Natl. Acad. Sci. USA 71, 2453-2455].

Bacteria↗
PubMed1984

Regulation of repressible acid phosphatase by cyclic AMP in Saccharomyces cerevisiae.

One of the cyr 1 mutants (cyr 1-2) in yeast produced low levels of adenylate cyclase and cyclic AMP at 25 degrees and was unable to derepress acid phosphatase. Addition of cyclic AMP to the cyr1-2 cultures elevated the level of repressible acid phosphatase activity. The bcy1 mutation, which suppresses the cyr1-2 mutation by allowing activity of a cyclic AMP-independent protein kinase, also allows acid phosphatase synthesis without restoring adenylate cyclase activity. The CYR3 mutant had structurally altered cyclic AMP-dependent protein kinase and was unable to derepress acid phosphatase. The cyr1 locus was different from pho2, pho4 and pho81, which were known to regulate acid phosphatase synthesis. Mutants carrying cyr1-2 and pho80, PHO81c, PHO82 or pho85 mutations, which confer constitutive synthesis of repressible acid phosphatase, produced acid phosphatase. The cyr1-2 mutant produced significantly low levels of invertase and alpha-D-glucosidase. These results indicated that cyclic AMP-dependent protein kinase exerts its function in the synthesis of repressible acid phosphatase and other enzymes.

Acid Phosphatase↗
PubMed1982

Synthesis of repressible acid phosphatase in Saccharomyces cerevisiae under conditions of enzyme instability.

The synthesis of repressible acid phosphatase in Saccharomyces cerevisiae was examined under conditions of blocked derepression as described by Toh-e et al. (Mol. Gen. Genet. 162:139-149, 1978). Based on a genetic and biochemical analysis of the phenomenon these authors proposed a new regulatory model for acid phosphatase expression involving a simultaneous interaction of regulatory factors in the control of structural gene transcription. We demonstrate here that under growth conditions that fail to produce acid phosphatase the enzyme is readily inactivated. Furthermore, we demonstrate under these conditions the production of acid phosphatase mRNA which is active both in vitro and in vivo in the synthesis of enzyme. This eliminates any step prior to translation of acid phosphatase polypeptide as an explanation for the phenomenon. We interpret our results for the block in appearance of acid phosphatase as a result of both deaccelerated growth and cellular biosynthesis during derepression, accompanied by an enhanced instability of the enzyme.

Acid Phosphatase↗
PubMed1977

Factors affecting the amount and the activity of the glutamate dehydrogenases of Coprinus cinereus.

Kinetic analyses done with cell-free extracts of this basidiomycete fungus showed that the NADP-linked glutamate dehydrogenase exhibited positively co-operative interactions with the substrates 2-oxoglutarate and NADPH, negatively co-operative kinetics with NADP+ and was extremely sensitive to inhibition of deamination activity by ammonium and/or ammonia. The NAD-linked enzyme showed positive co-operativity with NADH, Michaelis-Menten kinetics with all other substrates and was subject only to mild inhibitions by the reaction products. Considered together with the values of the Michaelis constants, these results indicate that the former enzyme is primarily concerned with the amination of 2-oxoglutarate when the concentration of this substrate exceeds about 4 mM, while the NAD-linked enzyme is able to aminate or deaminate as metabolic conditions require. Synthesis of both enzymes was repressed by addition of carbamyl phosphate or N-acetyl-glutamate to mycelial cultures growing in media containing glucose and ammonium as carbon and nitrogen sources. Growth in media containing urea results in repression of the NADP-linked glutamate dehydrogenase and derepression of the NAD-linked enzyme. Such results indicate a connexion between the glutamate dehydrogenases and the urea cycle. It is suggested that under normal conditions of growth on complex media nitrogen is assimilated in the form of amino acids and that the glutamate dehydrogenases act in support of transaminases to allow this process to continue, and in support of the urea cycle to allow the disposal of excess nitrogen.

Agaricales↗
PubMed1989

Proteolytic catabolite inactivation in Saccharomyces cerevisiae.

Fermentable sugars, when added to cells of Saccharomyces cerevisiae growing on a non-fermentable carbon source, cause repression of the synthesis of certain enzymes ("catabolite repression") and in addition inactivation of a smaller group of enzymes ("catabolite inactivation"). Enzymes for which "catabolite inactivation" has been observed are listed herein. In five cases, it has been shown that the mechanism of catabolite inactivation is proteolytic in nature. Our present knowledge on the conditions and the mechanisms of initiation of inactivation and the biological significance of the proteolytic inactivation is summarized for these five enzymes: cytoplasmic malate dehydrogenase, aminopeptidase I, fructose-1,6-bisphosphatase (FBPase), phosphoenolpyruvate carboxykinase and isocitrate lyase. With the exception of aminopeptidase I, these enzymes are key enzymes of gluconeogenesis in S. cerevisiae. It is obvious that gluconeogenesis is no longer necessary, if a fermentable carbon source is available.

Aminopeptidases↗
PubMed1984

A regulatory locus, Hdc-e, determines the response of mouse kidney histidine decarboxylase to estrogen.

Levels of histidine decarboxylase (HDC; EC 4.1.1.22) activity in female mouse kidney are modulated by estrogen (administered as implanted pellets). In some inbred strains HDC activity is induced by estrogen, while in others the enzyme is repressed. Immunoprecipitation with an anti-fetal rat HDC antiserum has shown that induction and repression of HDC levels are due to changes in enzyme concentration. Segregation analysis has identified a single additively inherited regulatory locus, Hdc-e, which determines the response to estrogen. The allele Hdc-eb (C57BL/10) determines induction, and the allele Hdc-ed (DBA/2) determines repression. Preliminary evidence indicates cosegregation of Hdc-e alleles with alleles of another regulatory locus, Hdc-c (determining kidney HDC concentration), and therefore putative linkage of Hdc-e with the HDC gene complex on chromosome 2. This is the first report of a mammalian regulatory gene controlling two opposite mechanisms, induction and repression in response to a single effector.

Animals↗