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The ribosomal binding domain for the bacterial release factors RF‐1, RF‐2 and RF‐3
Author(s) -
McCaughan Kim K.,
Ward Christina D.,
Trotman Clive N.A.,
Tate Warren P.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80576-1
Subject(s) - ribosome , ribosomal protein , escherichia coli , radio frequency , chemistry , biophysics , biology , microbiology and biotechnology , biochemistry , rna , gene , computer science , telecommunications
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.