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Gene Review:

tRNA-Gly - tRNA

Kazachstania servazzii

Mazauric, M.H. et al., Kern, D. et al., Romby, P. et al., Sibler, A.P. et al.

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Disease relevance of tRNA-Gly

The temperature-jump method was used to compare the stability of anticodon-anticodon duplexes formed by the self-association of two tRNAs: yeast tRNA-Asp and Escherichia coli tRNA-Gly [1].
tRNA glycylation system from Thermus thermophilus. tRNAGly identity and functional interrelation with the glycylation systems from other phylae [2].

High impact information on tRNA-Gly

Dimeric GlyRSs from mammalian and archaebacteria acylate efficiently only eukaryotic and archaebacterial tRNAGly with a discriminatory A73, whereas tetrameric Escherichia coli GlyRS acylates only eubacterial tRNAGly with a discriminatory U73 [2].
Addition of both tRNAGly and ATP.MgCl2 plus glycine displaced the equilibrium toward the dimeric form of the enzyme [3].
It is likely to be 5-carboxymethylaminomethyluridine. tRNA Gly and tRNA Pro have an unmodified uridine in the wobble position allowing the reading of all four codons of a four-codon family [4].
At neutral pH, it is found that only tRNA-Asp duplexes exist whereas at pH 5.0 only tRNA-Gly duplexes are formed [1].

References

Studies on anticodon-anticodon interactions: hemi-protonation of cytosines induces self-pairing through the GCC anticodon of E. coli tRNA-Gly. Romby, P., Westhof, E., Moras, D., Giegé, R., Houssier, C., Grosjean, H. J. Biomol. Struct. Dyn. (1986) [Pubmed]
tRNA glycylation system from Thermus thermophilus. tRNAGly identity and functional interrelation with the glycylation systems from other phylae. Mazauric, M.H., Roy, H., Kern, D. Biochemistry (1999) [Pubmed]
Glycyl-tRNA synthetase from baker's yeast. Interconversion between active and inactive forms of the enzyme. Kern, D., Giegé, R., Ebel, J.P. Biochemistry (1981) [Pubmed]
Codon reading patterns in Saccharomyces cerevisiae mitochondria based on sequences of mitochondrial tRNAs. Sibler, A.P., Dirheimer, G., Martin, R.P. FEBS Lett. (1986) [Pubmed]

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