Does unpaired adenosine-66 from helix II of Escherichia coli 5S RNA bind to protein L18?

@article{Christiansen1985DoesUA,
  title={Does unpaired adenosine-66 from helix II of Escherichia coli 5S RNA bind to protein L18?},
  author={Jette Christiansen and S. Douthwaite and Anni Christensen and Roger A. Garrett},
  journal={The EMBO journal},
  year={1985},
  volume={4 4},
  pages={1019-24}
}
Adenosine-66 is unpaired within helix II of Escherichia coli 5S RNA and lies in the binding site of ribosomal protein L18. It has been proposed as a recognition site for protein L18. We have investigated further the structural importance of this nucleotide by deleting it. The 5S RNA gene of the rrnB operon of E. coli was subjected to primer-directed mutagenesis. To produce the deletion it was necessary to use simultaneously the mutagenic dodecamer dCGGCGCACGGCG and the universal M13 primer… CONTINUE READING