Inhibition of isoleucyl-transfer ribonucleic acid synthetase in Echerichia coli by pseudomonic acid
نویسندگان
چکیده
منابع مشابه
Inhibition of isoleucyl-transfer ribonucleic acid synthetase in Escherichia coli by pseudomonic acid.
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 کاملRole 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...
متن کاملInteractions of tyrosyl transfer ribonucleic acid synthetase from Escherichia coli with its substrates. Inhibition by transfer ribonucleic acid.
Transfer RNA inhibited the tyrosine-dependent ATPpyrophosphate exchange catalyzed by tyrosyl-tRNA synthetase from IIscherichia coli. The inhibition was specific for tRNATY’; it was competitive with tyrosine and noncompetitive with ATP. tRNA modified by periodate oxidation or by limited digestion with phosphodiesterase proved to be a stronger inhibitor of the enzyme than native tRNA; the inhibit...
متن کاملInteraction of pseudomonic acid A with Escherichia coli B isoleucyl-tRNA synthetase.
Sodium pseudomonate was shown to be a powerful competitive inhibitor of Escherichia coli B isoleucyl-tRNA synthetase (Ile-tRNA synthetase). The antibiotic competitively inhibits (Ki 6 nM; cf. Km 6.3 microM), with respect top isoleucine, the formation of the enzyme . Ile approximately AMP complex as measured by the pyrophosphate-exchange reaction, and has no effect on the transfer of [14C]isoleu...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1978
ISSN: 0264-6021
DOI: 10.1042/bj1760305