title: The ribosomal binding domain for the bacterial release factors RF-1, RF-2 and RF-3.
abstract: The Escherichia coli ribosomal proteins, L7/L12, are dominant over L11 in modulating the binding of RF-1 and RF-2 to ribosomes. The elevated activity of RF-2 on L11-lacking ribosomes over those containing L11 is abolished by IgG against L7/L12 or by removing the L7/L12 proteins. Adding back L7/L12 restores the original phenotype. The stimulatory factor, RF-3, is active on ribosomes depleted of L7/L12 but on those which lack L11 the stimulatory effects are less pronounced or often not seen. RF-3 cannot restore activity with RF-1 or RF-2 to ribosomes lacking both these sets of proteins. The stimulatory effects of an absence of either L11 or RF-3 on the activity of RF-2 are not additive or synergistic.
mesh_terms: D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D009154:Mutation; D010454:Peptide Termination Factors / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
chemical_list: D010454:Peptide Termination Factors; D012269:Ribosomal Proteins; C041460:peptide chain termination release factor 2; C027624:ribosomal protein L11; C016700:ribosomal protein L7-L12