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T G Cooper

Publications and source records attributed to T G Cooper.

At least 289 records · Page 16Linked to original sources
PubMed1974

Inhibition of lacZ gene translation initiation in trp-lac fusion strains.

Different levels of beta-galactosidase are found in various trp-lac fusion strains. These levels of beta-galactosidase fall within a 60-fold range. The amount of thiogalactoside transacetylase activity detected in these same strains only varies 10-fold and is found in amounts greater than those predicted from the beta-galactosidase levels. The observation that the beta-galactosidase and thiogalactoside transacetylase levels are not directly proportional, that the lacZ messenger ribonucleic acid (mRNA) levels are not proportional to the beta-galactosidase activity, that, at least for the one fusion strain tested, the SuA polarity suppressor does not affect the beta-galactosidase level, and that, in all but one strain, the beta-galactosidase activity appears to reside in normal beta-galactosidase molecules suggests that the disproportionately low production of beta-galactosidase is due to a decrease in the frequency of translation initiation of lacZ mRNA in these strains. Several mechanisms are proposed to explain this decrease. Some possible bases for the disproportional production of beta-galactosidase and thiogalactoside transacetylase are also described. The preferred explanation for these disproportional enzyme levels is that only a fraction of the full complement of ribosomes need initiate translation at lacZ for the functional synthesis of lac mRNA to occur and that once the lac ribonucleic acid is made a full complement of ribosomes can bind at internal translation initiation sites at Y and A.

Acetyltransferases↗
PubMed1974

Oxaluric acid: a non-metabolizable inducer of the allantoin degradative enzymes in Saccharomyces cerevisiae.

Saccharomyces cerevisiae degrades allantoin in five steps to ammonia, CO(2), and glyoxylate. Previously we demonstrated that allophanic acid, the last intermediate of the pathway, was required for induction of all five degradative enzymes. The data presented here indicate that oxaluric acid, an allophanate analogue, is capable of serving as a non-metabolizable inducer. Oxaluric acid brings about a high level of induction even in strains lacking urea carboxylase. Induction observed with parabanic acid was found to result from its spontaneous breakdown to oxaluric acid.

Allantoin↗
PubMed1974

Nitrogen repression of the allantoin degradative enzymes in Saccharomyces cerevisiae.

Saccharomyces cerevisiae can utilize allantoin as a sole nitrogen source by degrading it to ammonia, "CO(2)," and glyoxylate. We have previously shown that synthesis of the allantoin degradative enzymes is contingent upon the presence of allophanate, the last intermediate in the pathway. The reported repression of arginase by ammonia prompted us to ascertain whether or not the allantoin degradative system would respond in a similar manner. We observed that the differential rates of allantoinase and allophanate hydrolase synthesis were not decreased appreciably when comparing cultures grown on urea to those grown on urea plus ammonia. These experiments were also performed using the strain and conditions previously reported by Dubois, Grenson, and Wiame. We found allophanate hydrolase production to be twofold repressed by ammonia when that strain was grown on glucose-urea plus ammonia medium. If, however, serine or a number of other readily metabolized amino acids were provided in place of ammonia, production of the allantoin degradative enzymes was quickly (within 20 min) and severely repressed in both strains. We conclude that repression previously attributed to ammonia may result from its metabolism to amino acids and other metabolites.

Alanine↗
PubMed1974

Clustering of the genes for allantoin degradation in Saccharomyces cerevisiae.

We have shown that allantoin degradation in Saccharomyces cerevisiae proceeds exclusively through the intermediate formation of allantoic acid, urea, and allophanic acid. The number of reactions between allantoic acid and urea, however, remains obscure owing to our inability to isolate a mutant defective in ureidoglycolate hydrolase. Structural genes for the enzymes, allantoinase (dal1) and allantoicase (dal2) are located on chromosome IX promixal to the centromere in the order dal1-dal2-lysl.

Allantoin↗
PubMed1973

Induction of the allantoin degradative enzymes in Saccharomyces cerevisiae by the last intermediate of the pathway.

Saccharomyces cerevisiae can degrade allantoin in five steps to glyoxylate, ammonia, and "CO(2)." We previously demonstrated that synthesis of the urea carboxylase-allophanate hydrolase multienzyme complex is contingent upon the presence of allophanic acid, the product of the urea carboxylase reaction. Since these enzymes catalyze the last two reactions of allantoin degradation, experiments were performed to establish whether or not the presence of allophanic acid was required for synthesis of any other enzymes participating in this degradative pathway. The data presented here indicate that allophanic acid is required for synthesis of all enzymes participating in allantoin degradation. This conclusion is based upon the observation that: (i) wild-type strains produced a large amount of allantoinase upon addition of allantoin, allantoate, ureidoglycolate, or urea to the medium, (ii) no increase in activity was observed unless the added compound could be metabolized to allophanate, (iii) strains lacking allophanate hydrolase contained large amounts of allantoinase even in the absence of added urea, and (iv) the urea analogue, formamide, was capable of inducing allantoinase synthesis in wild-type strains but would not serve this function in a strain lacking urea carboxylase.

Allantoin↗