Summary
The identification of ribosomal proteins that occur at, or near, the subunit interface of the 30S and 50S subunits in the E. coli 70S ribosome was attempted by studying the effect of antibodies on the Mg++ dependent dissociation-association equilibrium of 70S ribosomes. Dissociated ribosomes were mixed with monovalent fragments of IgG antibodies (Fab's) specific for each ribosomal protein and then reassociated into intact 70S particles. Various degrees of inhibition of this reassociation were observed for proteins S9, S11, S12, S14, S20, L1, L6, L14, L15, L19, L20, L23, L26 and L27. A small amount of aggregation of 50S subunits was caused by IgG's specific for the proteins S9, S11, S12, S14 and S20 and purified 50S subunits. It was inferred that the presence of small amounts of these proteins on 50S subunits was compatible with their presence at the subunit interface. Finally, the capacity of proteins S11 and S12 to bind to 23S RNA was demonstrated.
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Communicated by E. Bautz
Paper No. 84 on “Ribosomal Proteins”. Preceding paper is by Rahmsdorf et al., Molec. gen. Genet. 127, 259–271 (1973).
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Morrison, C.A., Garrett, R.A., Zeichhardt, H. et al. Proteins occurring at, or near, the subunit interface of E. coli ribosomes. Molec. Gen. Genet. 127, 359–368 (1973). https://doi.org/10.1007/BF00267106
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DOI: https://doi.org/10.1007/BF00267106