Studies on the binding of the ribosomal protein complex L7/12-L10 and protein L11 to the 5'-one third of 23S RNA: a functional centre of the 50S subunit.
The RNA binding sites of the protein complex of L7/12 dimers and L10, and of protein L11, occur within the 5'-one third of 23S RNA. Binding of the L7/12-L10 protein complex to the 23S RNA is stimulated by protein L11 and vice-versa. This is the second example to be established of mutual stimulation of RNA binding by two ribosomal proteins or protein complexes, and suggests that this may be an important principle governing ribosomal protein-RNA assembly. When the L7/12-L10 complex is bound to the RNA, L10 becomes strongly resistant to trypsin. Since the L7/12 dimer does not bind specifically to the 23S RNA, this suggests that L10 constitutes a major RNA binding site of the protein complex. Only one of the L7/12 dimers is bound strongly in the (L7/12-L10)-23S RNA complex; the other can dissociate with no concurrent loss of L10.
D004926:Escherichia coli / Q000032:analysis; D046911:Macromolecular Substances; D008970:Molecular Weight; D011485:Protein Binding; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D014357:Trypsin
D046911:Macromolecular Substances; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D014357:Trypsin