Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA.

@article{Guillier2005DoubleMM,
  title={Double molecular mimicry in Escherichia coli: binding of ribosomal protein L20 to its two sites in mRNA is similar to its binding to 23S rRNA.},
  author={Maude Guillier and Fr{\'e}d{\'e}ric Allemand and F. Dardel and Catherine A. Royer and Mathias Springer and Claude Chiaruttini},
  journal={Molecular microbiology},
  year={2005},
  volume={56 6},
  pages={1441-56}
}
Escherichia coli ribosomal L20 is one of five proteins essential for the first reconstitution step of the 50S ribosomal subunit in vitro. It is purely an assembly protein, because it can be withdrawn from the mature subunit without effect on ribosome activity. In addition, L20 represses the translation of its own gene by binding to two sites in its mRNA. The first site is a pseudoknot formed by a base-pairing interaction between nucleotide sequences separated by more than 280 nucleotides… CONTINUE READING

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