Studies on anticodon-anticodon interactions: hemi-protonation of cytosines induces self-pairing through the GCC anticodon of E. coli tRNA-Gly.

@article{Romby1986StudiesOA,
  title={Studies on anticodon-anticodon interactions: hemi-protonation of cytosines induces self-pairing through the GCC anticodon of E. coli tRNA-Gly.},
  author={Pascale Romby and Eric Westhof and Dino Moras and Richard Gieg{\'e} and Claude Houssier and Henri Grosjean},
  journal={Journal of biomolecular structure & dynamics},
  year={1986},
  volume={4 2},
  pages={193-203}
}
The temperature-jump method was used to compare the stability of anticodon-anticodon duplexes formed by the self-association of two tRNAs: yeast tRNA-Asp and Escherichia coli tRNA-Gly. Yeast tRNA-Asp duplexes contain a U/U mismatch while E. coli tRNA-Gly dimers have a C/C mismatch in the middle position of their quasi self-complementary anticodons GUC and GCC, respectively. At neutral pH, it is found that only tRNA-Asp duplexes exist whereas at pH 5.0 only tRNA-Gly duplexes are formed. This… CONTINUE READING