Identification of 50S Proteins at the Peptidyl-tRNA Binding Site of Escherichia coli Ribosomes
AUTOR(ES)
Oen, Helen
RESUMO
Bromoacetyl-phenylalanyl-tRNAphe 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-tRNAphe can participate in peptidebond formation with phenylalanyl-tRNAphe 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-tRNAphe 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-tRNAphe 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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=427112Documentos Relacionados
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