E coli tRNA coding for histidine GTG anti-codon
E. coli tRNA^His(GTG) is a 77-nucleotide transfer RNA that decodes CAC and CAU histidine codons via its GTG (GUG) anticodon and is aminoacylated by histidyl-tRNA synthetase (HisRS), a class IIa homodimeric enzyme. It adopts the canonical cloverleaf secondary structure and L-shaped tertiary fold, with a short variable loop characteristic of class I tRNAs. tRNA^His is unique among all tRNAs in carrying an additional guanosine at position −1 (G−1) at the 5' end of the acceptor stem, which is added post-transcriptionally by the enzyme tRNA^His guanylyltransferase (Thg1). This extra G−1 base, paired with the discriminator base C73, serves as the primary and essential identity element for HisRS recognition, a feature conserved across all domains of life and absent in all other tRNAs. The GTG anticodon also contributes to HisRS specificity, with anticodon bases directly contacting the C-terminal anticodon-binding domain of HisRS. Its highly distinctive aminoacylation identity rules and the universally conserved G−1 feature have made tRNA^His a central model for studying non-canonical tRNA identity, class IIa synthetase–tRNA recognition, and the evolutionary origins of the genetic code.
Applications -
1) RNAcentral ID: URS0000597E49_511145
2) Rosen, A. E., & Musier-Forsyth, K. (2004). "Recognition of G-1:C73 atomic groups by Escherichia coli histidyl-tRNA synthetase." Journal of the American Chemical Society, 126(1), 64–65
3) Francklyn, C., & Schimmel, P. (1990). "Enzymatic aminoacylation of an eight-base-pair microhelix with histidine." Proceedings of the National Academy of Sciences, 87(21), 8655–8659
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