Amino-terminal sequences of indoleglycerol phosphate synthetase of Escherichia coli and Salmonella typhimurium

Li, S S; Hanlon, Joan E.; Yanofsky, Charles

doi:10.1128/jb.123.2.761-764.1975

Cited by 6 publications

(2 citation statements)

References 24 publications

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“…An intermediate situation is known to occur in the B. subtilis trp operon where two adjacent genes, trpC and trpF, specify these two separate enzymes. All the available evidence from amino acid sequences indicates that the structural genes for each of the enzymes of the tryptophan pathway in the bacteria discussed are closely related (5,24,36). In contrast, it is quite clear that in every major bacterial group studied so far the chromosomal location of these genes, as well as the regulatory elements associated with them, differ widely.…”

Section: Resultsmentioning

confidence: 99%

Regulation of enzyme synthesis in the tryptophan pathway of Acinetobacter calcoaceticus

Cohn¹,

Crawford²

1976

J Bacteriol

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In Acinetobacter calcoaceticus the seven genes coding for the enzymes responsible for tryptophan synthesis map at three chromosomal locations. Two three-gene clusters, one (trpGDC) specifying the small subunit of anthranilate synthase, phosphoribosyl transferase, and indoleglycerol phosphate synthase and the other (trpFBA) specifying phosphoribosyl anthranilate isomerase and both tryptophan synthase subunits, are not linked to each other or to the trpE gene specifying the large anthranilate synthase subunit. When regulation of trp gene expression is studied in the wild type, only the level of the trpF gene product decreases upon addition of tryptophan to the medium. Tryptophan starvation of tryptophan auxotrophs, however, results in increased levels of all the tryptophan enzymes; this and additional evidence suggests that the expression of all the trp genes is subject to repression. The trpGDC genes are coordinately controlled, and the trpE gene is regulated in parallel with them. The trpFBA genes are controlled neither coordinately nor in parallel with the other trp genes, but respond proportionally when compared with each other. So far, two types of constitutive mutants have been found. The first class of mutants apparently occurs in the structural gene for a repressor protein; this repressor locus is unlinked to any of the biosynthetic trp genes and affects only the expression of trpE and the trpGDC cluster. The second class contains mutants closely linked to the trpGDC region; they overproduce only the gene products of this cluster.

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Section: Resultsmentioning

confidence: 99%

Regulation of enzyme synthesis in the tryptophan pathway of Acinetobacter calcoaceticus

Cohn¹,

Crawford²

1976

J Bacteriol

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“…However, we have also found that InGP synthetase activity in S. typhimurium but not in E. coli is derepressed by the tryptophan analog 3-indolylacrylic acid ( 22), suggesting that the E. coli but not the S. typhimurium enzyme is unstable under these conditions. Differences in stability of the activities could be due to differences in the primary sequence of the two proteins (18). Roth, and B. N. Ames.…”

Section: Discussionmentioning

confidence: 99%

Inactivation and partial degradation of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase in nongrowing cultures of Escherichia coli

Mosteller¹,

Nishimoto²,

Goldstein³

1977

J Bacteriol

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The stability of tryptophan biosynthetic enzyme activities was examined in cultures of repressor-negative (trpR) strains of Escherichia coli K-12 incubated under conditions of nutrient starvation of chloramphenicol inhibition. The results show that four of the five activities examined are stable under most nongrowing conditions, whereas one activity, indoleglycerol phosphate (InGP) synthetase, carried by the trpC protein, is unstable under most conditions tested. Phosphoribosylanthranilate (PRA) isomerase activity, which is also carried by the trpC protein, is unstable during starvation for ammonium, cysteine, or sulfate but is stable under other nongrowing conditions where InGP synthetase is not. InGP synthetase activity but not PRA isomerase activity is also diminished about twofold in cultures using glycerol as a carbon-energy source. These results indicate that one or both activities of the trpC protein is specifically inactivated under several culture conditions. Experiments with antibodies to the trpC protein show that sulfate-starved and ammonium-starved cultures contain 20 to 40% less immunologically reactive trpC protein than unstarved cultures. This indicates that the trpC protein is probably partially degraded under these conditions. During recovery from sulfate starvation or ammonium starvation, cultures slowly regain normal levels of InGP synthetase and PRA isomerase activities, suggesting that inactivation may be reversible.

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A functional hybrid ribosome binding site in tryptophan operon messenger RNA of Escherichia coli

Christie

Platt

1980

Journal of Molecular Biology

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Amino-terminal sequences of indoleglycerol phosphate synthetase of Escherichia coli and Salmonella typhimurium

Abstract: The partial sequences of the first 40 residues of indoleglycerol phosphate synthetase of Escherichia coli and Salmonella typhimurium were determined, and three amino acid differences were observed among the 38 residues compared.

Cited by 6 publications

References 24 publications

Regulation of enzyme synthesis in the tryptophan pathway of Acinetobacter calcoaceticus

Regulation of enzyme synthesis in the tryptophan pathway of Acinetobacter calcoaceticus

Inactivation and partial degradation of phosphoribosylanthranilate isomerase-indoleglycerol phosphate synthetase in nongrowing cultures of Escherichia coli

A functional hybrid ribosome binding site in tryptophan operon messenger RNA of Escherichia coli

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