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RNA modifications in the anticodon region of tRNAs play a critical role in establishing such non-universal genetic codes.
2
The domain I (corresponding to the anticodon stem of tRNA) is a rigid three alpha-helix bundle.
3
The post-transcriptional modifications of tRNA's anticodon domain are the most diverse and chemically complex of any RNA modifications.
4
Certain stress conditions can induce cleavage of tRNAs around the anticodon loop via the use of the ribonuclease angiogenin.
5
All three aa-tRNAs have the same 'loaded spring' conformation with a kink and twist between the D-stem and anticodon stem.
6
Reversing this structural change in the tRNA anticodon by addition of excess exogenous queuine reversed the 6-thioguanine-induced growth inhibition and differentiation.
7
Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half.
8
Nucleotide modifications within the anticodon are found in the majority of all tRNAs and are among the last maturation events to occur in vivo.
9
These data suggest that competition between unrelated aminoacyl-tRNA synthetases for overlapping anticodon sequences is a determinant of the phylogenetic distribution of extant synthetase families.