CHLORAMPHENICOL-PROMOTED REPRESSION OF Β-Galactosidase SYNTHESIS IN ESCHERICHIA COLI

Sypherd, Paul S.; Strauss, Norman

doi:10.1073/pnas.49.3.400

Cited by 43 publications

(22 citation statements)

References 9 publications

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“…The effects of CAP described here are clearly different from the effects of CAP demonstrated by Sypherd et al (29)(30)(31)(32) and Paigen (25). Those authors showed that the same low levels of CAP preferentially inhibited depression of j3-galactosidase and OTCase, but only in exponentially growing cultures (29).…”

contrasting

confidence: 85%

“…We have observed enhanced synthesis of the same enzymes, but only in starved cultures. The preferential inhibition by CAP could also be obtained with other antibiotic protein synthesis inhibitors and other nutritional manipulations (30,32), but enhanced synthesis was specifically induced by CAP. Thus, in spite of intriguing similarities between the two sets of observations, there is no evidence that the two effects are mediated through similar mechanisms.…”

mentioning

confidence: 96%

“…Sypherd et al (30,32) and Paigen (25) have shown that the synthesis of ,3-galactosidase and other inducible enzymes was inhibited to a far greater extent than total protein synthesis when Escherichia coli cells were induced while growing in the presence of low concentrations (0.5 to 1.0 ,g/ml) of CAP.…”

mentioning

confidence: 99%

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Stimulation of Derepressed Enzyme Synthesis in Bacteria by Growth on Sublethal Concentrations of Chloramphenicol

Ford

Switzer

1975

Antimicrob Agents Chemother

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Culturing of Salmonella typhimurium or Escherichia coli cells in the presence of low concentrations (≤1 μg/ml) of chloramphenicol (CAP) permitted exponential growth, but at doubling times up to twice those of controls. When such cultures were subsequently starved for uracil or arginine, derepression of aspartate transcarbamylase (ATCase) or ornithine transcarbamylase, respectively, was enhanced three- to 10-fold as compared to cultures not exposed to CAP. Enhancement of β-galactosidase synthesis by prior exposure to CAP was also observed in uracil-starved E. coli cultures. Stimulation of enzyme synthesis appeared to be a specific effect of CAP; low levels of erythromycin, puromycin, sparsomycin, tetracycline, and rifampin did not show such effects. Derepression of ATCase synthesis in exponentially growing cells in the presence of CAP did not result in stimulation of enzyme synthesis by CAP. A prior history of growth of a culture in the presence of CAP was shown to be necessary for enhancement of enzyme synthesis by CAP; furthermore, continued presence of CAP in the medium during starvation was not necessary for enhanced enzyme synthesis and inhibited it in some instances. Enhanced enzyme synthesis in starving, CAP-treated cultures could be blocked by rifampin, which suggested that CAP treatment allows prolonged or more extensive messenger ribonucleic acid synthesis.

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confidence: 85%

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confidence: 96%

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Stimulation of Derepressed Enzyme Synthesis in Bacteria by Growth on Sublethal Concentrations of Chloramphenicol

Ford

Switzer

1975

Antimicrob Agents Chemother

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“…system (Sypherd, Strauss & Treffers, 1962), where the antibiotics act by inhibiting the inducer-promoted synthesis of rnessenger-RNA (Sypherd & Strauss, 1963 (Fig. 3).…”

Section: Resultsmentioning

confidence: 99%

Induction of an Anthranilate Oxidation System During the Metabolism of ortho-Nitrobenzoate by Certain Bacteria

Cain¹

1966

Journal of General Microbiology

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SUMMARYNocardia opaca, a flavobacterium and certain other bacteria, when grown on o-nitrobenzoate, accumulated anthranilate in the medium in the early stages of growth. The subsequent disappearance of this metabolite in growing cultures was always correlated with the appearance of an anthranilate oxidase system in the organisms. This phenomenon has the features of a typical enzyme adaptation except that the inducer is a byproduct of the cells' own metabolism; hence it has been termed 'metabolite induction '. The results confirm previous suggestions that, in these micro-organisms, anthranilate is not an obligatory intermediate in the direct energy-producing pathway of o-nitrobenzoate breakdown but is produced in a side reaction.

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“…Horowitz and Kohlmeyer (9) showed that the extent to which f-galactosidase synthesis was inhibited by 5-fluorouracil depended on the carbon source in the medium, and assumed that catabolite repression may play a role in the inhibition of 3-galactosidase. Chloramphenicolpromoted inhibition of 3-galactosidase was assumed to be due to inhibition of lac mRNA synthesis and to inhibition of some later steps in protein synthesis (19).…”

mentioning

confidence: 99%

Catabolite Repression in Inhibition of β-Galactosidase Synthesis by Escherichia coli in the Presence of Agents Producing Translation Errors

Artman

Werthamer

Gelb

1972

Antimicrob Agents Chemother

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CHLORAMPHENICOL-PROMOTED REPRESSION OF Β-Galactosidase SYNTHESIS IN ESCHERICHIA COLI

Cited by 43 publications

References 9 publications

Stimulation of Derepressed Enzyme Synthesis in Bacteria by Growth on Sublethal Concentrations of Chloramphenicol

Stimulation of Derepressed Enzyme Synthesis in Bacteria by Growth on Sublethal Concentrations of Chloramphenicol

Induction of an Anthranilate Oxidation System During the Metabolism of ortho-Nitrobenzoate by Certain Bacteria

Catabolite Repression in Inhibition of β-Galactosidase Synthesis by Escherichia coli in the Presence of Agents Producing Translation Errors

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