Interrelation between Transfer RNA and Amino-Acid-Activating Sites of Methionyl Transfer RNA Synthetase from Escherichia coli
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منابع مشابه
The 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...
متن کاملThe recognition of methionine analogues by Escherichia coli methionyl-transfer ribonucleic acid synthetase.
Bronskill, P., Kennedy, T. D. & Lane, B. G. (1972) Biochim. Biophys. Acta 262,275-282 Dunn, D. B. (1963) Biochem. J. 8 6 , 1 4 ~ 1 5 ~ Dunn, D. B. & Flack, I. H. (1967) Abstr. FEBS Meet. 4th pp. 82 Dunn, D. B. & Flack, I. H. (1970) John Innes Institute Annual Report 61,7678 Fissekis, J. D. & Sweet, F. (1970) Biochemistry 9, 3136-3142 Gray, M. W. & Lane, B. G. (1968) Biochemistry 7,3441-3453 Ken...
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Due to its long half-life compared to messenger RNA, bacterial transfer RNA is known as stable RNA. Here, we show that tRNAs become highly unstable as part of Escherichia coli's response to amino acid starvation. Degradation of the majority of cellular tRNA occurs within twenty minutes of the onset of starvation for each of several amino acids. Both the non-cognate and cognate tRNA for the amin...
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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...
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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: European Journal of Biochemistry
سال: 1977
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1977.tb11825.x