E coli tRNA coding for Asparagine GTT anti-codon
E. coli tRNA-Asn (GTT) is the transfer RNA responsible for decoding AAU and AAC asparagine codons during translation. It is charged exclusively by asparaginyl-tRNA synthetase (AsnRS), a Class II aminoacyl-tRNA synthetase. AsnRS recognition of tRNA-Asn is critically dependent on the anticodon, particularly positions U35 and U36, which are individually essential identity elements; their importance is further underscored by the fact that the closely related Class I LysRS, where present, also competes for U35/U36, shaping the phylogenetic distribution of synthetase families across bacteria. A distinctive biochemical feature of tRNA-Asn is the presence of queuosine (Q), a hypermodified 7-deazaguanosine derivative bearing a cyclopentenediol side chain, at the wobble position 34 of its anticodon. This modification, first structurally characterized in E. coli tRNA-Asn, tRNA-Asp, tRNA-His, and tRNA-Tyr, enhances decoding accuracy at U-ending codons and is biosynthesized exclusively by bacteria, making it a key microbiome-dependent modification in higher eukaryotes. While the listed tRNA does not possess the modification, it serves as a useful control tRNA for structure-function studies. The D-stem and D-loop of tRNA-Asn share close sequence homology with E. coli tRNA-Asp, reflecting an ancestral relationship between these two tRNA families.
Applications:
1) RNAcentral ID: URS000008CEF9_511145
2) Ohashi, K., Harada, F., Ohashi, Z., Nishimura, S., Stewart, T. S., Vogeli, G., McCutchan, T., & Soll, D. (1976). The nucleotide sequence of asparagine tRNA from Escherichia coli. Nucleic Acids Research, 3(12), 3369–3376
3) Kasai, H., Oashi, Z., Harada, F., Nishimura, S., Oppenheimer, N. J., Crain, P. F., Liehr, J. G., von Minden, D. L., & McCloskey, J. A. (1975). Structure of the modified nucleoside Q isolated from Escherichia coli transfer ribonucleic acid. Biochemistry, 14(19), 4198–4208
4) Söll, D., Becker, H. D., Plateau, P., Blanquet, S., & Ibba, M. (2000). Context-dependent anticodon recognition by class I lysyl-tRNA synthetases. Proceedings of the National Academy of Sciences, 97(26), 14224–14228
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