title: Sequence-specific interaction of R17 coat protein with its ribonucleic acid binding site.
abstract: The interaction between phage R17 coat protein and its RNA binding site for translational repression was studied as an example of a sequence-specific RNA--protein interaction. Nuclease protection and selection experiments define the binding site to about 20 contiguous nucleotides which form a hairpin. A nitrocellulose filter retention assay is used to show that the binding between the coat protein and a synthetic 21-nucleotide RNA fragment conforms to a simple bimolecular reaction. Unit stoichiometry and a Kd of about 1 nM are obtained at 2 degrees C in buffer containing 0.19 M salt. The interaction is highly sequence specific since a variety of RNAs failed to compete with the 21-nucleotide fragment for coat protein binding.
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D001667:Binding, Competitive; D002213:Capsid / Q000378:metabolism*; D036022:Capsid Proteins; D003090:Coliphages / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism; D009690:Nucleic Acid Conformation; D012367:RNA, Viral / Q000378:metabolism*; D016601:RNA-Binding Proteins; D014764:Viral Proteins / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; D012367:RNA, Viral; D016601:RNA-Binding Proteins; D014764:Viral Proteins