Escherichia coli ribosomal protein S1 has two polynucleotide binding sites.

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Abstract
The interaction of S. coli ribosomal protein S1 with a variety of RNA and DNA oligomers and polymers was studied, using a sedimentation technique and the quenching of intrinsic protein fluorescence upon nucleic acid binding to obtain equilibrium binding parameters. Two polynucleotide binding sites were detected on S1: site I binds single-stranded DNA or RNA and does not discriminate between adenine- and cytidine-containing polynucleotides, while site II binding is highly specific for RNA over DNA and shows a marked preference for cytidine polynucleotides over the corresponding adenine-containing species. The binding properties of S1 to denatured DNA cellulose and poly(rC)-cellulose showed that every S1 molecule carries a site I and site II. Some possible implications of these results for mechanisms of protein synthesis and phage Q.beta. replication are briefly considered.