Immunochemical accessibility of ribosomal protein S4 in the 30 S ribosome. The interaction of S4 with S5 and S12.
The reactivity of protein S4-specific antibody preparations with 30 S ribosomal subunits and intermediates of in vitro subunit reconstitution has been characterized using a quantitative antibody binding assay. Anti-S4 antibody preparations did not react with native 30 S ribosomal subunits; however, they did react with various subunit assembly intermediates that ... lacked proteins S5 and S12. The inclusion of proteins S5 and S12 in reconstituted particles resulted in a large decrease in anti-S4 reactivity, and it was concluded that proteins S5 and S12 are primarily responsible for the masking of S4 antigenic determinants in the 30 S subunit. The effect of S5 and S12 on S4 accessibility is consistent with data from a variety of other approaches, suggesting that these proteins form a structural and functional domain in the small ribosomal subunit.
Mesh Terms:
Antibodies, Bacterial, Bacterial Proteins, Binding Sites, Antibody, Electrophoresis, Agar Gel, Epitopes, Escherichia coli, Geobacillus stearothermophilus, Immune Sera, Immunodiffusion, Macromolecular Substances, Ribosomal Proteins, Ribosomes
Antibodies, Bacterial, Bacterial Proteins, Binding Sites, Antibody, Electrophoresis, Agar Gel, Epitopes, Escherichia coli, Geobacillus stearothermophilus, Immune Sera, Immunodiffusion, Macromolecular Substances, Ribosomal Proteins, Ribosomes
J. Mol. Biol.
Date: Apr. 05, 1983
PubMed ID: 6188845
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