Role of Isoleucyl-Transfer Ribonucleic Acid Synthetase in Ribonucleic Acid Synthesis and Enzyme Repression in Yeast
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منابع مشابه
Role of isoleucyl-transfer ribonucleic acid synthetase in ribonucleic acid synthesis and enzyme repression in yeast.
Temperature-sensitive mutations in the isoleucyl-transfer ribonucleic acid (tRNA) synthetase of yeast, ilS(-)1-1 and ilS(-)1-2, were used to examine the role of aminoacyl-tRNA synthetase enzymes in the regulation of ribonucleic acid (RNA) synthesis and enzyme synthesis in a eucaryotic organism. At the permissive temperature, 70 to 100% of the intracellular isoleucyl-tRNA was charged in mutants ...
متن کاملTransfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase.
When incubated with the appropriate substrates, purified Escherichia coli isoleucyl ribonucleic acid synthetase can form a complex with either isoleucylor valyladenylate which may be isolated by Sephadex filtration. Whereas the isoleucyladenylate complex reacts with transfer RNA (tRNA) to form isoleucyl-RNA, the valyladenylate complex breaks down in the presence of tRNA. In place of transacylat...
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The mode of action of the antibiotic pseudomonic acid has been studied in Escherichia coli. Pseudomonic acid strongly inhibits protein and RNA synthesis in vivo. The antibiotic had no effect on highly purified DNA-dependent RNA polymerase and showed only a weak inhibitory effect on a poly(U)-directed polyphenylalanine-forming ribosomal preparation. Chloramphenicol reversed inhibition of RNA syn...
متن کاملTransfer Ribonucleic Acid Synthetase in Escherichia colil
The valyl-transfer ribonucleic acid (tRNA) synthetase of Escherichia coli strain NP2907, previously described as having an elevated Km for adenosine triphosphate and reduced stability in vitro compared to the wild type, was found to be conditionally thermolabile in vivo. The rate of inactivation of this enzyme at a particular temperature appears to be coordinated with the rate of growth; at 40 ...
متن کاملThe activation of arginyl transfer ribonucleic acid synthetase by transfer ribonucleic acid.
The arginine-activating enzyme of Escherichk coli requires transfer ribonucleic acid (tRNA) for catalysis of the ATP-pyrophosphate exchange reaction. Only the specific arginiie-accepting tRNA is effective5 and the terminal adenylic acid residue is essential for the reaction. A previously described isotope-trapping experiment led to the suggestion that an arginyl-tRNA ester was not formed during...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1969
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.100.2.579-584.1969