E coli tRNA coding for arginine ACG anti-codon
E. coli tRNA-Arg (ACG) is a 77-nucleotide transfer RNA that decodes CGU arginine codons during translation. It is one of multiple tRNA-Arg isoacceptors in E. coli, encoded by four genomic loci (argQ, argY, argV, and argZ). It is charged by arginyl-tRNA synthetase (ArgRS), a Class I aminoacyl-tRNA synthetase that is unusual in requiring its cognate tRNA for the first step of amino acid activation, a tRNA-dependent adenylation mechanism, not seen in most other Class I aaRSs. The primary identity determinants for ArgRS recognition are the second and third anticodon bases (C35 and G36 or U36) and the conserved A20 in the variable pocket of the D-loop; the discriminator base at position 73 plays an auxiliary role. Structural studies of the E. coli ArgRS–tRNA^Arg complex at 3.0 Å resolution revealed that A20 from the D-loop is the pivotal docking element, contacting five ArgRS residues in a recognition mode not previously observed in other aaRS–tRNA complexes, with additional contacts from U20a and U16 stabilizing the interaction.
Applications:
1) RNAcentral ID: URS0000349C05_511145
2) Tamura, K., Himeno, H., Asahara, H., Hasegawa, T. & Shimizu, M. (1992). In vitro study of E. coli tRNA(Arg) and tRNA(Lys) identity elements. Nucleic Acids Res. 20(9):2335–2339
3) Stephen, P., Ye, S., Zhou, M., Song, J., Zhang, R., Wang, E.-D., Giegé, R. & Lin, S.-X. (2018). Structure of Escherichia coli arginyl-tRNA synthetase in complex with tRNA: pivotal role of the D-loop. J. Mol. Biol. 430(11):1590–1606
4) Delagoutte, B., Moras, D. & Cavarelli, J. (2000). tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding. EMBO J. 19(21):5599–5610 RCSB PDB: 1F7V
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