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：1971
卷号：68
期号：12
页码：3163-3167
DOI：10.1073/pnas.68.12.3163
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Escherichia coli and rabbit reticulocyte (f[3H]Met-tRNA{middle dot}AUG{middle dot}ribosome) intermediates undergo hydrolysis, with release of f[3H]methionine, upon addition of tRNA or CpCpA in the presence of acetone. This ribosomal catalyzed reaction has similar requirements, pH optimum, and antibiotic sensitivity to those of peptidyl transferase. Two antibiotics, lincomycin with E. coli ribosomes and anisomycin with reticulocyte ribosomes, inhibit peptide-bond formation and transesterification activities of peptidyl transferase, but stimulate hydrolysis of f[3H]Met-tRNA. Earlier studies have suggested peptidyl transferase activity is essential for R factor-dependent hydrolysis of f(3H)Met-tRNA. These studies indicate that peptidyl transferase has the capacity for f(3H)Met-tRNA hydrolysis and, therefore, may be responsible for peptidyl-tRNA cleavage during peptide chain termination.
关键词：reticulocytes ; E. coli ; anisomycin ; R factors ; lincomycin
