Abstract
A mutation of Salmonella typhimurium was obtained that results in the failure of cells to synthesize the enzyme l-histidine ammonia-lyase (histidase). The mutation mapped within the hutH gene and in merodiploid strains was dominant over the wild-type allele. Extracts from cells bearing the trans-dominant histidase-negative allele were shown to contain material that reacts immunologically with antiserum against purified wild-type histidase. It is proposed that the trans-dominant allele results in the synthesis of defective histidase subunits that can combine with, and partially inactivate, wild-type histidase subunits. This subunit mixing presumably does occur, as the enzyme synthesized in a hybrid merodiploid strain is abnormally heat sensitive.
MeSH Terms
Alleles
Ammonia-Lyases/biosynthesis
Ammonium Sulfate
Animals
Buffers
Centrifugation, Density Gradient
Chromatography
Chromatography, DEAE-Cellulose
Chromosome Mapping
Chromosomes, Bacterial
Culture Media
Deoxyribonucleases
Histidine Ammonia-Lyase/analysis,biosynthesis,immunology
Hot Temperature
Mutation
Rabbits/immunology
Rubidium
Salmonella Phages
Salmonella typhimurium/enzymology,growth & development,immunology,isolation & purification
Urocanate Hydratase/analysis
Chemicals
Buffers
Culture Media
Deoxyribonucleases
Urocanate Hydratase
Ammonia-Lyases
Histidine Ammonia-Lyase
Rubidium
Ammonium Sulfate
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hagen D C
Lipton P J
Magasanik B
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