Changes in the conformation and stability of 5 S RNA upon the binding of ribosomal proteins.
The binding of ribosomal proteins L25, L18, and L5 to 5 S RNA results in a conformational change and a destabilization of the 5 S RNA molecule. The changes observed in the near ultraviolet circular dichroism (CD) spectra and in the melting profiles indicate an increase in base stacking uith an accompanying increase in asymmetry of the bases and a decrease in the conformational stability of the 5 S RNA. These results are consistent with the interpretation that the binding of these proteins increases the stacking of specific single-stranded bases in 5 S RNA and aligns them in helical arrays, resulting in a conformation which facilitates base-pairing with nucleotide segment(s) of the ribosomal 23 S RNA or the transfer RNA (or both). The simple and precise difference CD method described here is potentially useful for studying subtle conformational changes of other nucleic acid-protein interactions.
D001426:Bacterial Proteins; D002942:Circular Dichroism; D004926:Escherichia coli; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012329:RNA, Bacterial; D012269:Ribosomal Proteins
D001426:Bacterial Proteins; D012329:RNA, Bacterial; D012269:Ribosomal Proteins