Molding a peptide into an RNA site by in vivo peptide evolution.

  title={Molding a peptide into an RNA site by in vivo peptide evolution.},
  author={Kyuya Harada and Shelley S. Martin and Ruoying Tan and Alan D. Frankel},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={94 22},
Short peptides corresponding to the arginine-rich domains of several RNA-binding proteins are able to bind to their specific RNA sites with high affinities and specificities. In the case of the HIV-1 Rev-Rev response element (RRE) complex, the peptide forms a single alpha-helix that binds deeply in a widened, distorted RNA major groove and makes a substantial set of base-specific and backbone contacts. Using a reporter system based on antitermination by the bacteriophage lambda N protein, it… CONTINUE READING


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Harada et al

  • C. Woffendin, U. Ranga, +4 authors 2889–2894. 11892 Biochemistry
  • Proc. Natl. Acad. Sci. USA 94
  • 1997
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