Abstract
The interaction of Escherichia coli ribosomal protein S1 with a variety of RNA and DNA oligomers and polymers has been studied, using both a sedimentation technique and the quenching of intrinsic protein fluorescence upon nucleic acid binding to obtain equilibrium binding parameters. Two polynucleotide binding sites have been detected on S1: site I binds either single-stranded DNA or RNA and does not discriminate between adenine- and cytidine-containing polynucleotides, while the II binding is highly specific for RNA over DNA and shows a marked preference for cytidine polynucleotides over the corresponding adenine-containing species. On the basis of the binding properties of S1 to denatured DNA cellulose and poly(rC)-cellulose, it is demonstrated that every S1 molecule carries both a site I and a site II. Some possible implications of these results for mechanisms of protein synthesis and phage Qbeta replication are briefly considered.
MeSH Terms
Bacterial Proteins/metabolism
Binding Sites
Centrifugation, Density Gradient
DNA, Bacterial/metabolism
Escherichia coli/metabolism,ultrastructure
Polynucleotides/metabolism
RNA, Bacterial/metabolism
Ribosomal Proteins/metabolism
Spectrometry, Fluorescence
Chemicals
Bacterial Proteins
DNA, Bacterial
Polynucleotides
RNA, Bacterial
Ribosomal Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Draper D E
Pratt C W
von Hippel P H
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