PMID:9586030
| Citation |
Nameki, N, Tamura, K, Asahara, H and Hasegawa, T' (1997) Recognition of tRNA(Gly) by three widely diverged glycyl-tRNA synthetases: evolution of tRNA recognition. Nucleic Acids Symp. Ser. ':123-4 |
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| Abstract |
Glycyl-tRNA synthetase (GlyRS) is an unusual aminoacyl-tRNA synthetase because it varies in its quarternary structure between organisms; Escherichia coli GlyRS is an alpha 2 beta 2 tetramer, whereas those of Thermus thermophilus and yeast are alpha 2 dimers. In contrast, the tRNA(Gly) sequence is virtually identical in E. coli and T. thermophilus but very different in yeast. In this study, we examined the molecular recognition of tRNA(Gly) by three widely diverged GlyRSs using in vitro tRNA transcripts. The results obtained in the mutation studies indicate that despite such large differences of the two prokaryotic GlyRSs, tRNA(Gly) identity has been essentially conserved in prokaryotes, and that there are also differences in the acceptor stem recognition between prokaryotes and yeast. The clear separation between prokaryotes and yeast is retained in the identity element location, whereas the apparent diversity of the two prokaryotic enzymes does not reflect on the tRNA recognition. |
| Links | |
| Keywords |
Base Sequence; Conserved Sequence; Dimerization; Escherichia coli/enzymology; Evolution, Molecular; Glycine-tRNA Ligase/chemistry; Glycine-tRNA Ligase/metabolism; Macromolecular Substances; Mutagenesis; Protein Conformation; RNA, Transfer, Gly/chemistry; RNA, Transfer, Gly/metabolism; Saccharomyces cerevisiae/enzymology; Substrate Specificity; Thermus thermophilus/enzymology; Transcription, Genetic |
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