Abstract
Proteins L7 and L12 from 50S ribosomal subunits of Escherichia coli are required for peptidechain termination. This termination process is inhibited by thiostrepton. Since both thiostrepton-treated ribosomes and those depleted of L7 and L12 have a markedly reduced ability to form release factor·UA[3H]A·ribosome complexes, the binding of release factors to the ribosome appears to be the primary site of inhibition.
Keywords: E. coli, thiostrepton, ribosomal protein
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