Evidence for the existence of two arginyl-transfer ribonucleic acid synthetase activities in Escherichia coli.
نویسندگان
چکیده
Two arginyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.13, arginine: ribonucleic acid ligase adenosine monophosphate) activities were found in extracts of Escherichia coli strains AB1132 and NP2. The two arginyl-tRNA synthetase activities in extracts of strain AB1132 were found to be separable by diethylaminoethyl-cellulose column chromatography, Sephadex column fractionation, and by sucrose density gradient centrifugation. In addition, in the standard assay using extracts of strain AB1132 there were two pH optima for arginyl-tRNA synthetase activity. Furthermore, when arginyl-tRNA synthetase of strain NP2 was fractionated by hydroxylapatite column chromatography, two activities were observed which were similar to those of strain AB1132.
منابع مشابه
Control of arginine biosynthesis in Escherichia coli: inhibition of arginyl-transfer ribonucleic acid synthetase activity.
In this study, we have extended our earlier observations indicating in vitro inhibition of arginyl-transfer ribonucleic acid synthetase (EC 6.1.13, arginine: soluble ribonucleic acid ligase, adenosine monophosphate) activity by the arginine biosynthetic precursors ornithine, citrulline, and argininosuccinate. Furthermore, we report evidence which suggest that this enzyme activity is inhibited b...
متن کاملThe arginyl transfer ribonucleic acid synthetase of Escherichia coli.
The arginyl transfer ribonucleic acid (tRNA) synthetase of Escherichia coli has been purified over SO&fold. Its kinetic properties are similar to those of other amino acidactivating enzymes; it has a pH optimum near 8 and does not react with amino acids that occur in proteins other than arginine, but the analogues homoarginine and canavanine are competitive inhibitors, and canavanine can be est...
متن کاملInhibition of arginyl-transfer ribonucleic acid synthetase activity of Escherichia coli by arginine biosynthetic precursors.
The arginine biosynthetic precursors, ornithine, citrulline, and argininosuccinate, inhibit arginyl-transfer ribonucleic acid (tRNA) synthetase (EC 6.1.1.13, arginine: soluble RNA ligase, adenosine monophosphate) activity in the in vitro attachment assay system. Ornithine is the most potent, argininosuccinate is next, and citrulline is least effective. The implications of these results are disc...
متن کاملMutants of Escherichia coli K-12 with an altered glutamyl-transfer ribonucleic acid synthetase.
Three streptomycin-suppressible lethal mutants of Escherichia coli K-12 have been shown to possess structurally altered glutamyl-transfer ribonucleic acid (tRNA) synthetases. Each mutant synthetase displays a K(m) value for glutamate which is 10-fold higher than the parental value, and the mutations reside in two widely separate loci on the genetic map. Mixing of the mutant extracts in pairs ga...
متن کاملRepression of enzymes of arginine biosynthesis by L-canavanine in arginyl-transfer ribonucleic acid synthetase mutants of Escherichia coli.
We show that the arginine analogue, l-canavanine, repressed the accumulation of translatable messenger ribonucleic acid (RNA) for three arginine biosynthetic enzymes in Escherichia coli. The method used to determine the level of translatable messenger RNA depended upon measurement of a burst of enzyme synthesis as described previously. E. coli strains with defective arginyltransfer ribonucleic ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bacteriology
دوره 113 2 شماره
صفحات -
تاریخ انتشار 1973