The requirement for ribosomal proteins L7 and L12 in peptide-chain termination.
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[(3)H]A.ribosome complexes, the binding of release factors to the ribosome appears to be the primary site of inhibition.
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001426:Bacterial Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D008715:Methionine / Q000378:metabolism; D010443:Peptide Chain Termination, Translational / Q000187:drug effects*; D010454:Peptide Termination Factors; D010455:Peptides / Q000494:pharmacology; D012333:RNA, Messenger / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000378:metabolism*; D014316:Tritium
D000900:Anti-Bacterial Agents; D001426:Bacterial Proteins; D010454:Peptide Termination Factors; D010455:Peptides; D012333:RNA, Messenger; D014316:Tritium; D008715:Methionine