Escherichia coli ribosomal 5S RNA-protein L25 nucleoprotein complex: effects of RNA binding on the protein structure and the nature of the interaction.
The complexes of three variants of Escherichia coli 5S RNA with ribosomal protein L25 have been studied by high-field proton nuclear magnetic resonance. A spectroscopic method is demonstrated to help distinguish the macromolecular sources of proton resonances in nucleoprotein complexes. The effects of L25 binding on the three RNAs tested were small; the presence of the L25 did not strongly influence the conformation of the RNA. The interaction of L25 with 5S RNA produced modest, but distinctive, alterations in the protein spectrum, in both the aromatic region and the upfield spectrum. As judged by these changes, the mechanism of binding was the same in all three cases. The changes seen in the spectrum of L25 indicate that its conformation is not altered in a major way upon RNA binding. Arginine residues appear to be involved in the binding mechanism. Intercalation of L25 aromatic residues with RNA bases does not appear to play a role in the interaction.
D004926:Escherichia coli / Q000378:metabolism*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011485:Protein Binding; D011487:Protein Conformation; D012335:RNA, Ribosomal / Q000378:metabolism*; D012261:Ribonucleoproteins / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000378:metabolism*
D012335:RNA, Ribosomal; D012261:Ribonucleoproteins; D012269:Ribosomal Proteins; C031127:ribosomal protein L25