Journal of Molecular Biology
Regular articleRecognition of tRNAGly by three widely diverged glycyl-tRNA synthetases1
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Cited by (39)
Interchangeable parts: The evolutionarily dynamic tRNA population in plant mitochondria
2020, MitochondrionCitation Excerpt :This was surprising because prokaryotic and eukaryotic GlyRSs use a specific nucleotide identity at position 73 for activity, which is different between the two (nuclear and mitochondrial) tRNA-Gly genes (Giegé et al., 1998). This ability for the organellar, bacterial-like GlyRS to recognize cytosolic tRNA-Gly suggests the evolution of expanded substrate recognition based on comparisons with the GlyRS from Escherichia coli, which has limited activity on cytosolic tRNA substrates (Duchêne et al., 2001; Nameki et al., 1997). More generally, data from Arabidopsis thaliana on tRNA gene content in the mitogenome and subcellular localization of aaRSs provide multiple examples supporting both of the evolutionary scenarios described above (Duchêne et al., 2009).
Glycyl-tRNA synthetase from Nanoarchaeum equitans: The first crystal structure of archaeal GlyRS and analysis of its tRNA glycylation
2019, Biochemical and Biophysical Research CommunicationsCitation Excerpt :These enzymes are classified into two groups according to the structure of the catalytic domain: class I enzymes, containing a Rossmann fold with two signature sequences (HIGH and KMSKS), and class II enzymes, containing antiparallel β-sheets with three conserved motifs [9,10]. Glycyl-tRNA synthetase (GlyRS) belongs to the class II group of aminoacyl-tRNA synthetases, which includes two widely divergent oligomeric types [11–13]: a dimeric (α2) species, present in archaea, eukaryotes, and some bacteria; and a heterotetrameric form (α2β2), present in most bacteria. Previous studies showed that the anticodon binding domains of dimeric and tetrameric GlyRSs are non-homologous and that the anticodon binding domain of tetrameric GlyRS was likely fused to the C-terminal of the β-subunit during evolution [14].
On the role of an unusual tRNA<sup>Gly</sup> isoacceptor in Staphylococcus aureus
2009, BiochimieCitation Excerpt :When we compared this unusual tRNA with the previously known as non-proteinogenic tRNAGly isoacceptors from S. epidermidis we observed that their sequences are highly similar (Fig. S1). The few observed differences between the two species are not conserved and are located in positions that do not seem to affect the recognition by GlyRS or to differentiate EF-Tu binding capacity, according to what has been previously reported [18–20,22,24]. However, tRNAs participating in bacterial cell wall synthesis might contain different idiosyncratic features as has been recently described for tRNAAla in Weissella viridescens [25].
Overlapping Destinations for Two Dual Targeted Glycyl-tRNA Synthetases in Arabidopsis thaliana and Phaseolus vulgaris
2001, Journal of Biological Chemistry
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Edited by D. E. Draper