Accessibility of Isoleucyl Transfer Ribonucleic Acid to Solvent during Recognition by Isoleucyl Transfer Ribonucleic Acid Synthetase
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Transfer 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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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 ...
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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...
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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...
متن کاملThe aminoacylation of transfer ribonucleic acid. Recognition of methionine by Escherichia coli methionyl-transfer ribonucleic acid synthetase.
The mechanism of the recognition of methionine by Escherichia coli methionyl-tRNA synthetase was examined by a kinetic study of the recognition of methionine analogues in the ATP-PPi exchange reaction and the tRNA-aminoacylation reaction. The results show that the recognition mechanism consists of three parts: (1) the recognition of the size, shape and chemical nature of the amino acid side cha...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45273-3