A cyanogen bromide fragment of S4 that specifically rebinds 16S RNA

• Published in: Nucleic acids research Vol. 15; no. 24; pp. 10331 - 10343
• Main Authors: CONRAD, R. C, CRAVEN, G. R
• Format: Journal Article
• Language: English
• Published: Oxford Oxford University Press 23.12.1987
• Subjects: Biological and medical sciences; Cell structures and functions; Chloroplast, photosynthetic membrane and photosynthesis; Cyanogen Bromide; Escherichia coli; Fundamental and applied biological sciences. Psychology; Molecular and cellular biology; Peptide Fragments - metabolism; Protein Binding; Ribosomal Proteins - metabolism; Ribosomes - ultrastructure; RNA, Ribosomal - metabolism; RNA, Ribosomal, 16S - metabolism; Structure-Activity Relationship; Ribosome; Peptide fragment; Ribosomal RNA; Supramolecular structure; 16S-RNA; Bacteria; Molecular interaction; Ribosomal protein
• ISSN: 0305-1048; 1362-4962
• DOI: 10.1093/nar/15.24.10331

Escherichia coli ribosomal protein S4 was subjected to cyanogen bromide cleavage and was found to generate a complete cleavage product capable of rebinding 16S rRNA. This fragment, consisting of residues 1-103, was found to bind with an apparent association constant of 11 microM-1. This fragment was used in place of S4 in an in vitro reconstitution experiment. Although the particles formed had a protein composition not significantly different from reconstituted 30S ribosomal subunits, their sedimentation behavior was more like that of particles reconstituted without S4. These results indicate to us that, although residues 104-203 of S4 are involved in the assembly of the 30S ribosome, they are not necessary for the binding of S4 to 16S RNA. Taken with previous results, the domain of S4 involved in specific binding of 16S RNA can be confined to residues 47-103.