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PMID: 6383864 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The ribosomal binding domain for the bacterial release factors RF-1, RF-2 and RF-3.

FEBS letters ·Vol. 175 ·No. 1 ·1984-09-17 ·Pages 90-4

McCaughan KK, Ward CD, Trotman CN, Tate WP

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
Binding Sites Escherichia coli/metabolism Kinetics Mutation Peptide Termination Factors/metabolism Ribosomal Proteins/metabolism Ribosomes/metabolism
Chemicals
Peptide Termination Factors Ribosomal Proteins peptide chain termination release factor 2 ribosomal protein L11 ribosomal protein L7-L12
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
McCaughan K K
Ward C D
Trotman C N
Tate W P
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1984-09-17
Pages
90-4
Language
English
Region
England
NLM ID
0155157
Subset
IM
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