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Nucleic Acids Research, 1984, Vol. 12, No. 5 2499-2508
© 1984

MOLECULAR BIOLOGY

The modelling of the decoding site of the Escherichia coli ribosome

Tago Sarapuu, Ene Utsav* and Richard Villems

Laboratory of Molecular Genetics, Institute of Chemical Physics and Biophysics 14/16 Kingissepa Street, 202400 Tartu, Estonian SSR, USSR *Laboratory of Molecular Biology, Tartu State University 14/16 Kingissepa Street, 202400 Tartu, Estonian SSR, USSR

Received December 5, 1983. Accepted February 9, 1984.

Individual ribosomal proteins S4, S9 and S13 were tested for their ability to interact with tRNA and synthetic polynucleotides. All three proteins bind to imobilized to Sepharose poly(A) and poly(U), while S4 and S13 form stoichiometric (1:1) complexes with tRNA in solution. We show that only the polynucleotide complexes are able to select their cognate tRNAs. In particular, the affinity of tRNAPhe to the binary poly(U).S13 complex is about three orders of magnitude higher than that for poly(U) alone.


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