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. 1973 Oct;70(10):2799-803.
doi: 10.1073/pnas.70.10.2799.

Identification of 50S proteins at the peptidyl-tRNA binding site of Escherichia coli ribosomes

H Oen, M Pellegrini, D Eilat, C R Cantor

Identification of 50S proteins at the peptidyl-tRNA binding site of Escherichia coli ribosomes

H Oen et al. Proc Natl Acad Sci U S A. 1973 Oct.

Abstract

Bromoacetyl-phenylalanyl-tRNA(phe) bound to 70S E. coli ribosomes reacts covalently with proteins of the 50S subunit. The major reactions are with proteins L2 and L27. In the presence of poly(U), 70S-bound bromoacetyl-phenylalanyl-tRNA(phe) can participate in peptidebond formation with phenylalanyl-tRNA(phe) or puromycin. Most of the products of these reactions are also found covalently attached to L2 and L27. Chloramphenicol and sparsomycin markedly inhibit the peptide-bond formation. These results strongly suggest that bromoacetylphenylalanyl-tRNA(phe) can function as a normal peptidyl-tRNA and that the 50S proteins, L2 and L27, are located in the peptidyl-tRNA binding site. The side reactions of bromoacetyl-phenylalanyl-tRNA(phe) are with one or more 50S proteins from the set L14-17, L6 and/or L11, and L26. These occur to a much less extent than the reactions with L2 and L27. Any functional significance of the side reactions is unknown.

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References

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