Mapping hisS, the structural gene for histidyl-transfer ribonucleic acid synthetase, in Escherichia coli.
نویسندگان
چکیده
The structural gene for histidyl-tRNA synthetase was localized to 53.8 min on the Escherichia coli genome. The gene order in this region was determined to be dapE-purC-upp-purG-(guaA, guaB)-hisS-glyA.
منابع مشابه
Regulation of histidyl-transfer ribonucleic acid synthetase formation in a histidyl-transfer ribonucleic acid synthetase mutant of Salmonella typhimurium.
Control of formation of the histidyl-transfer ribonucleic acid (tRNA) synthetase with an increased K(m) for histidine was studied in a hisS mutant of Salmonella typhimurium. Histidine restriction of both the hisS and hisS(+) strains resulted in a derepression of synthesis of histidyl-tRNA synthetase. When grown in a concentration less than the K(m) (100 mug/ml) of l-histidine, the hisS mutant m...
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The histidyl-tRNA synthetase gene (hisS) from Streptococcus equisimilis was cloned and sequenced. The gene for this aminoacyl-tRNA synthetase has an open reading frame of 1278 nucleotides. The deduced amino acid sequence encodes a protein of 426 amino acids with MW = 47,932. The protein is predicted to be soluble with a pl = 5.27. The protein sequence has extensive overall identity/similarity w...
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The regulation of formation of histidyl-transfer ribonucleic acid (tRNA) synthetase was examined in strains of Salmonella typhimurium. When the first of the histidine-forming enzymes was wild type, the presence of 2-thiazolealanine in the growth medium prevented repression of histidyl-tRNA synthetase formation elicited by the addition of 1, 2, 4-triazole-3-alanine to these cultures. Conversely,...
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Two threonine-requiring mutants with derepressed expression of the threonine operon were isolated from an Escherichia coli K-12 strain containing two copies of the thr operon. One of them carries a leaky mutation in ilvA (the structural gene for threonine deaminase), which creates an isoleucine limitation and therefore derepression of the thr operon. In the second mutant, the enzymes of the thr...
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عنوان ژورنال:
- Journal of bacteriology
دوره 138 1 شماره
صفحات -
تاریخ انتشار 1979