Defining a smaller RNA substrate for elongation factor Tu.

@article{Nazarenko1995DefiningAS,
  title={Defining a smaller RNA substrate for elongation factor Tu.},
  author={I A Nazarenko and O. C. Uhlenbeck},
  journal={Biochemistry},
  year={1995},
  volume={34 8},
  pages={2545-52}
}
A nuclease protection assay was used to obtain equilibrium dissociation constants of Thermus thermophilus EF-Tu with two well-characterized internal deletions of Escherichia coli Ala-tRNA(Ala) and yeast Phe-tRNA(Phe). Aminoacylated tRNAs with the anticodon hairpin substituted by a tetranucleotide bind to EF-Tu as well as the corresponding full-sized tRNAs. However, the Ala minihelix, where residue A7 is joined directly to A49, binds to EF-Tu less well than the full-sized Ala-tRNA(Ala). Similar… CONTINUE READING