Summary
The site-specific complex formed between 16S RNA and the 30S ribosomal protein S4 from Escherichia coli has been degraded with pancreatic ribonuclease. We have recovered the nuclease-resistant RNA from this complex; we call it S4aR. S4aR will bind to S4, but it will not bind to the other 30S proteins that can form site-specific complexes with 16S RNA. The data presented here as well as elsewhere (Schaup et al., 1971b) show that S4aR has a mass of about 150000 daltons and that it is made up of several separate RNA fragments, each of which enters the complex with S4. We conclude that S4 interacts with several separate binding sites on the RNA and that these probably contain a great deal of double stranded structure.
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Communicated by H. G. Wittmann
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Schaup, H.W., Kurland, C.G. Molecular interactions of ribosomal components. Molec. Gen. Genet. 114, 350–357 (1972). https://doi.org/10.1007/BF00267503
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DOI: https://doi.org/10.1007/BF00267503