Identification of Chloramphenicol-Binding Protein in Escherichia coli Ribosomes by Affinity Labeling*

AUTOR(ES)

Pongs, Olaf

RESUMO

Monoiodoamphenicol, a synthetic analogue of chloramphenicol, has been shown by competition experiments with chloramphenicol and lincomycin to bind at the same site of 70S ribosomes as chloramphenicol. At — 2° it forms a 1:1 complex with 70S ribosomes having a value of K (7.5 × 104 M-1) that is one order of magnitude lower than that of chloramphenicol. At 37°, monoiodoamphenicol irreversibly inhibits the protein-synthesizing activity of E. coli ribosomes. It is shown that the analogue reacted preferentially with protein L16 of E. coli 70S ribosomes, and we therefore conclude that protein L16 belongs to the chloramphenicol-binding site of E. coli ribosomes.

Documentos Relacionados

• Identification of the Chloramphenicol-Binding Protein in Escherichia coli Ribosomes by Partial Reconstitution*
• Identification by Photo-Affinity Labeling of the Proteins in Escherichia coli Ribosomes Involved in Elongation Factor G-Dependent GDP Binding
• Identification of Heparin-binding Sites in Proteins by Selective Labeling*
• Inhibition of [14C]Chloramphenicol Binding to Escherichia coli Ribosomes by Erythromycin Derivatives
• Location of protein S1 of Escherichia coli ribosomes at the 'A'-site of the codon binding site. Affinity labeling studies with a 3'-modified A-U-G analog.