Evidence for Catabolite Degradation in the Glucose‐Dependent Inactivation of Yeast Cytoplamic Malate Dehydrogenase

Neeff, Jürgen; Hägele, Edger; Nauhaus, Jutta; Heer, Ursual; Mecke, Dieter

doi:10.1111/j.1432-1033.1978.tb12399.x

Cited by 53 publications

(23 citation statements)

References 26 publications

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“…This conclusion would be supported by the observation that in a yeast transformed with the FBP gene under the control of the PHO5 promoter, FbPase accumulates even in the presence of glucose, suggesting that an increase in the level of FbPase had saturated the inactivating system [20]. Catabolite inactivation accompanied by a specific loss of antigenic material has been shown to occur with other enzymes: phosphoenoipyruvate carboxykinase (PEPCK) [21][22][23] and malic dehydrogenase (MDH) [24,25]. To test whether these enzymes are degraded by the same system as FbPase, their inactivation was measured in the same strains.…”

Section: Resultssupporting

confidence: 53%

Regulation of yeast fructose‐1,6‐bisphosphatase in strains containing multicopy plasmids coding for this enzyme

1988

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The structural gene for yeast fructose-1,6-bisphosphatase (FbPase) has been cloned by complementation of a strain carrying the fbpl-1 mutation and lacking FbPase activity. By Northern analysis it could be shown that the fbpl-I mutation does not interfere with the transcription of the gene although no normal active enzyme is produced. Strains transformed with the cloned gene on a multicopy plasmid overproduce FbPase but are still subject to strong catabolite repression.Catabolite inactivation, however, is slowed down in such strains.

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Section: Resultssupporting

confidence: 53%

Regulation of yeast fructose‐1,6‐bisphosphatase in strains containing multicopy plasmids coding for this enzyme

1988

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“…The catabolite inactivation of gluconeogenic enzymes of Saccharomyces cerevisiae was shown to be accompanied by a loss of material immunochemically related to the enzymes [6,15,16], and the same was found for the inactivation of the NAD-and NADP-dependent glutamate dehydrogenases [5,17]. Definite proof for proteolysis would be obtained by the elucidation of the mechanism and by the isolation of protease mutants with altered inactivation.…”

Section: Discussionmentioning

confidence: 92%

“…Our results demonstrate that the loss of enzyme activity during the in vivo inactivation is accompanied by a decrease in cross-reactive material. This suggests that allantoinase is subject to proteolytic degradation during carbon starvation [4][5][6].…”

Section: Introductionmentioning

confidence: 99%

Allantoinase from Pseudomonas aeruginosa Purification, properties and immunochemical characterization of its in vivo inactivation

Janssen

Smits

Drift

1982

Biochimica et Biophysica Acta (BBA) - General Subjects

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The catabolic enzyme allantoinase is rapidly inactivated in cells of Pseudomonas aeruginosa when the stationary phase of growth is reached. This process is irreversible since the protein synthesis inhibitor chloramphenicol completely blocked the reappearance of allantoinase activity that is observed when allantoin is added to stationary cells. Purified allantoinase appeared to be a protein composed of four identical subunits with a molecular weight of 38000. With antibodies raised against purified allantoinase it was found that allantoinase inactivation is accompanied by a parallel decrease in immunologically reactive material. This suggests that ailantoinase inactivation is caused or followed by rapid proteolysis.

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“…Among gluconeogenetic enzymes, fructosebisphosphatase [3], cytoplasmic malate dehydrogenase [4,5] and phosphoenolpyruvate carboxykinase [6] have been reported to underly catabolite inactivation in Saccharomyces crrevisiue. Two different mechanisms have been shown to be involved in the inactivation of these enzymes: proteolysis for cytoplasmic inalate dehydrogenase [7,8] and phosphoenolpyruvate carboxykinase [9], and a rapid covalent modification followed by proteolysis for fructose-bisphosphatase [I 0, 111. Little is known about the identity of mediators of inactivation; Duntze et al [12] and Gancedo and Gancedo [I31 have suggested that metabolites formed in the first step of glycolysis may be responsible for initiation of cytoplasmic malate dehydrogenase inactivation.…”

mentioning

confidence: 99%

Effect of Caffeine on Glucose‐Induced Inactivation of Gluconeogenetic Enzymes in Saccharomyces cerevisiae

Tortora¹,

Burlini²,

Hanozet³

et al. 1982

European Journal of Biochemistry

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The mechanism of catabolite inactivation of three gluconeogenetic enzymes, fructose-l,6-bisphosphatase, cytoplasmic malate dehydrogenase and phosphoenolpyruvate carboxykinase, has been studied in the yeast Saccharomyces cerevisiae. The glucose-induced inactivation of the three enzymes is remarkably retarded by preincubation of the cells with different caffeine concentrations; however, a full conservation of activity has never been obtained, even at the highest drug concentration. Caffeine modifies the metabolic effects produced in the yeast cell by exposure to glucose. It reduces the consumption rate of glucose; changes the glycolytic intermediate pattern, giving rise to a crossover point at the level of the phosphofructokinase/fructose-bisphosphatase cycle; and increases the ATP level and the energy charge. Moreover, it substantially reduces the peak of intracellular cAMP content that immediately follows glucose entry; the magnitude of this effect is dependent on the drug concentration. The effect on the change of intracellular cAMP level appears, among all metabolic effects determined by caffeine, the only plausible one to explain the interference with catabolite inactivation of enzymes. Actually a strong negative correlation between residual activity of each of the three investigated enzymes and intracellular cAMP level has been demonstrated. The existence of a common mechanism of action of CAMP, as the mediating factor for catabolite inactivation of all three enzymes, is proposed.

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Evidence for Catabolite Degradation in the Glucose‐Dependent Inactivation of Yeast Cytoplamic Malate Dehydrogenase

Cited by 53 publications

References 26 publications

Regulation of yeast fructose‐1,6‐bisphosphatase in strains containing multicopy plasmids coding for this enzyme

Regulation of yeast fructose‐1,6‐bisphosphatase in strains containing multicopy plasmids coding for this enzyme

Allantoinase from Pseudomonas aeruginosa Purification, properties and immunochemical characterization of its in vivo inactivation

Effect of Caffeine on Glucose‐Induced Inactivation of Gluconeogenetic Enzymes in Saccharomyces cerevisiae

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