Sulfur-Deficient Transfer Ribonucleic Acid in a Cysteine-Requiring, “Relaxed” Mutant of Escherichia coli
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چکیده
منابع مشابه
Unusual valyl-transfer ribonucleic acid synthetase mutant of Escherichia coli.
Escherichia coli strain NP2907 was isolated as a spontaneous mutant of strain NP29, which possesses a thermolabile valyl-transfer ribonucleic acid (tRNA) synthetase. The valyl-tRNA synthetase of the new mutant, unlike that of its immediate parent, retains enzymatic activity in vitro but differs from the wild-type enzyme in stability and apparent K(m) for adenosine triphosphate. The new mutant l...
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The inability of the methionine requiring Escherichia coli mutant (1-344) to grow in methionine free media containing inorganic sulfur, cystine, or homocystine has been demonstrated (Lampen et al., 1947). While methionine has been shown to be essential for growth, the metabolism of nonmethionine sulfur added to media containing methionine has not been investigated directly. In the results repor...
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Escherichia coli strain 9D3 possesses a highly temperature-sensitive valyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.9). Since 9D3 is a rel(+) strain, it cannot carry out net RNA synthesis at high temperature. A 100-mug amount of chloramphenicol (CAP) per ml added in the absence of valine cannot stimulate RNA synthesis. Either 300 mug of CAP or 100 mug of CAP plus 50 mug of valine p...
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A mutant of Escherichia coli that lacks leucyl-, phenylalanyl-transfer ribonucleic acid-protein transferase had diminished activities of L-phenylalanyl-transfer ribonucleic acid synthetase and tryptophanase, grew faster than its parent with aspartic acid as the sole nitrogen source, accumulated higher levels of enterochelin in the medium during iron limitation, and exhibited an abnormal morphol...
متن کاملGlutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli
Escherichia coli glutamyl transfer ribonucleic acid synthetase acylates the three homologous tRNAGIU isoacceptors with very similar K, values (2.4 to 4.6 X lop7 M). The pure enzyme forms a 1: 1 complex with its cognate tRNA as judged by gradient centrifugation and fluorescence-quenching studies. The biological specificity of complex formation is not strictly observed in vitro since fluorescence...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1969
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.100.3.1322-1327.1969