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Start Over Topic genes Journal journal of bacteriology
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1. Gene expression after transformation of Bacillus subtilis.

Author

Chasin LA and Magasanik B

Subjects
Crosses, Genetic, Culture Media, DNA, Bacterial, Electrophoresis, Glucose, Histidine metabolism, Lyases metabolism, Mutation, Paper, Spectrophotometry, Tritium, Bacillus subtilis enzymology, Bacillus subtilis growth & development, Genes, Lyases biosynthesis, Transformation, Genetic
Abstract

Sensitive assays of histidase activity were used to follow the production of this enzyme as directed by a gene newly introduced into cells of Bacillus subtilis by transformation. Histidase activity can be detected in histidase-negative recipient cells within 1 hr after the addition of deoxyribonucleic acid extracted from histidase-positive donors. Enzyme production continues for one to two additional hours and then ceases. Histidase production in the transformed cells is fully sensitive to catabolite repression. Catabolite repression is rapidly established after transformation of recipient cells that are resistant to this form of regulation.

Published
1970
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2. Two mutations in the first gene of the histidine operon of Salmonella typhimurium affecting control.

Author

Rothman-Denes L and Martin RG

Subjects
Amino Acids pharmacology, Aspartic Acid metabolism, Aspartic Acid pharmacology, Chromosome Mapping, Culture Media, Drug Resistance, Microbial, Enzyme Repression, Genetics, Microbial, Histidine pharmacology, Microbial Sensitivity Tests, Models, Theoretical, Operon, Paper, Phosphotransferases antagonists & inhibitors, Phosphotransferases metabolism, Recombination, Genetic, Salmonella typhimurium drug effects, Salmonella typhimurium enzymology, Salmonella typhimurium growth & development, Salmonella typhimurium isolation & purification, Spectrophotometry, Transduction, Genetic, Triazoles, Genes, Histidine metabolism, Molecular Biology, Mutation, Salmonella typhimurium metabolism
Abstract

Two strains with mutations in the first structural gene of the histidine operon of Salmonella typhimurium were characterized. (The first structural gene specifies the first enzyme of histidine biosynthesis, phosphoribosyltransferase, which is sensitive to feedback inhibition by histidine.) One mutation, hisG3934, results in a phosphoribosyltransferase which is no longer sensitive to feedback inhibition by histidine but is instead subject to inhibition by aspartic acid. The other mutation, hisG3935, allows the histidine operon to be partially repressed by several amino acids, including aspartic acid. Analysis of hisG3935 is consistent with the hypothesis that phosphoribosyltransferase is directly involved in the regulation of the histidine operon.

Published
1971
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3. Biosynthesis of the Iron-Transport Compound Enterochelin: Mutants of Escherichia coli Unable to Synthesize 2,3-Dihydroxybenzoate

Author

I. G. Young, L Langman, Frank Gibson, and R. K. J. Luke

Subjects
Electrophoresis, Genetics, Microbial, Paper, Cyclohexanecarboxylic Acids, Ultraviolet Rays, Physiology and Metabolism, Iron, Mutant, Catechols, Shikimic Acid, Dehydrogenase, Biology, Iron Chelating Agents, medicine.disease_cause, Benzoates, Microbiology, Cell-free system, Serine, chemistry.chemical_compound, Biosynthesis, Transduction, Genetic, Escherichia coli, medicine, Molecular Biology, Cell-Free System, Structural gene, Chromosome Mapping, Shikimic acid, Molecular biology, Culture Media, Genes, Biochemistry, chemistry, Mutation, Indicators and Reagents
Abstract

Mutants of Escherichia coli K-12 blocked in each of the three enzymatic reactions between chorismate and 2,3-dihydroxybenzoate, in the pathway leading to the iron-sequestering compound enterochelin, have been isolated and biochemically characterized. The three genes concerned (designated entA, entB and entC ) have been shown to be clustered on the chromosome between purE and gal and to be located near minute 14 by cotransduction with the purE, lip , and fep genes. entA, entB , and entC were shown to be the structural genes for 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase, 2,3-dihydro-2,3-dihydroxybenzoate synthetase, and isochorismate synthetase, respectively.

Published
1971

4. Gene Expression After Transformation in Bacillus subtilis

Author

Lawrence A. Chasin and Boris Magasanik

Subjects
DNA, Bacterial, Electrophoresis, Paper, Catabolite repression, Lyases, Genetics and Molecular Biology, Bacillus subtilis, Biology, Tritium, medicine.disease_cause, Microbiology, chemistry.chemical_compound, Transformation, Genetic, Gene expression, medicine, Histidine, Molecular Biology, Gene, Crosses, Genetic, chemistry.chemical_classification, Mutation, biology.organism_classification, Culture Media, Transformation (genetics), Glucose, Enzyme, Genes, Biochemistry, chemistry, Spectrophotometry, DNA
Abstract

Sensitive assays of histidase activity were used to follow the production of this enzyme as directed by a gene newly introduced into cells of Bacillus subtilis by transformation. Histidase activity can be detected in histidase-negative recipient cells within 1 hr after the addition of deoxyribonucleic acid extracted from histidase-positive donors. Enzyme production continues for one to two additional hours and then ceases. Histidase production in the transformed cells is fully sensitive to catabolite repression. Catabolite repression is rapidly established after transformation of recipient cells that are resistant to this form of regulation.

Published
1970