HYDROLYSIS OF FMET TRANSFER RNA BY PEPTIDYL TRANSFERASE
HYDROLYSIS OF FMET TRANSFER RNA BY PEPTIDYL TRANSFERASE
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DOI:
10.1073/pnas.68.12.3163
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发表时间:
1971-01-01
影响因子:
11.1
通讯作者:
ROSMAN, M
中科院分区:
文献类型:
--
作者:
CASKEY, CT;BEAUDET, AL;ROSMAN, M
Escherichia coliand rabbit reticulocyte (f[3H]Met-tRNA·AUG·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 withE. coliribosomes 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.