期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：10
页码：2799-2803
DOI：10.1073/pnas.70.10.2799
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
关键词：protein L2 and L27 ; affinity labeling ; protein synthesis ; two-dimensional electrophoresis ; antibiotics
