Work

Identification of 50S Proteins at the Peptidyl-tRNA Binding Site of Escherichia coli Ribosomes

Year: 1973

Type: article

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.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.70.10.2799

Authors: Helen Oen, Maria Pellegrini, Dan Eilat, Charles R. Cantor

Institutions: Hebrew University of Jerusalem, Columbia University

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, National Institutes of Health, U.S. Public Health Service

OpenAlex ID: W2015562604

FWCI: 4.283

Cites: 16

Cited by: 43

Related to: 10