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Gene Review:

tRNA-Arg - tRNA

Kazachstania servazzii

Reyes, V.M. et al., Bacha, H. et al., Auxilien, S. et al., Cavarelli, J. et al., Fender, A. et al., et al.

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Disease relevance of tRNA-Arg

In yeast, inosine is found at the first position of the anticodon (position 34) of seven different isoacceptor tRNA species, while in Escherichia coli it is present only in tRNAArg [1].

High impact information on tRNA-Arg

While ArgRS requires tRNAArg for the first step of the aminoacylation reaction, the results show that its presence is not a prerequisite for L-arginine binding [2].
We found that site-directed mutation of the highly conserved C at position 56 to a G in the tRNAArg gene suppresses all transcription and does not activate the tRNAAsp gene [3].
PIVB RNA mainly contained tRNAArg (51.8%), tRNALys (17.1%), and tRNAHis (9.2%) which together accounted for 78% of the total PIVB tRNA [4].
A second endonuclease cleavage of pre-tRNAArg generates the mature 5' terminus of tRNAArg [5].
In the case of the phenylalanyl system, the crucial role of the wybutine residue (adjacent to the anticodon) in the activation of phenylalanyl-tRNA synthetase by the tRNA core has been analysed by comparison with native or modified non-cognate tRNAs (tRNATyr, tRNAArg) [6].

Associations of tRNA-Arg with chemical compounds

No arginyl adenylate is detectable as an intermediate in the aminoacylation of tRNAArg [7].
The latent aspartate acceptor capacity in a contemporary tRNAArg leads to the proposal of an evolutionary link between tRNA4Arg and tRNAAsp genes [8].

Other interactions of tRNA-Arg

Rescue of tRNAAsp gene transcription is effected either by the precise deletion of both the tRNAArg gene and spacer or by the precise deletion of this gene with concomitant introduction of an artificial RNA polymerase III start site in the spacer [3].

Analytical, diagnostic and therapeutic context of tRNA-Arg

Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes [9].

References

Mechanism, specificity and general properties of the yeast enzyme catalysing the formation of inosine 34 in the anticodon of transfer RNA. Auxilien, S., Crain, P.F., Trewyn, R.W., Grosjean, H. J. Mol. Biol. (1996) [Pubmed]
L-arginine recognition by yeast arginyl-tRNA synthetase. Cavarelli, J., Delagoutte, B., Eriani, G., Gangloff, J., Moras, D. EMBO J. (1998) [Pubmed]
Mutational analysis of the coordinate expression of the yeast tRNAArg-tRNAAsp gene tandem. Reyes, V.M., Newman, A., Abelson, J. Mol. Cell. Biol. (1986) [Pubmed]
Interaction of RNA with transformed glucocorticoid receptor. II. Identification of the RNA as transfer RNA. Ali, M., Vedeckis, W.V. J. Biol. Chem. (1987) [Pubmed]
Nucleolytic processing of a tRNAArg-tRNAAsp dimeric precursor by a homologous component from Saccharomyces cerevisiae. Engelke, D.R., Gegenheimer, P., Abelson, J. J. Biol. Chem. (1985) [Pubmed]
Conformational activation of aminoacyl-tRNA synthetases upon binding of tRNA. A facet of a multi-step adaptation process leading to the optimal biological activity. Bacha, H., Renaud, M., Lefevre, J.F., Remy, P. Eur. J. Biochem. (1982) [Pubmed]
No arginyl adenylate is detectable as an intermediate in the aminoacylation of tRNAArg. Thiebe, R. Eur. J. Biochem. (1983) [Pubmed]
A yeast arginine specific tRNA is a remnant aspartate acceptor. Fender, A., Geslain, R., Eriani, G., Giegé, R., Sissler, M., Florentz, C. Nucleic Acids Res. (2004) [Pubmed]
Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes. Delagoutte, B., Keith, G., Moras, D., Cavarelli, J. Acta Crystallogr. D Biol. Crystallogr. (2000) [Pubmed]

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