The Binding Site of Protein L1 on 23‐S Ribosomal RNA of Escherichia coli

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Abstract
Ribonucleoproteins were prepared by [T1] RNase [EC 3.1.4.8] digestion of a reconstituted complex of ribosomal protein L1 and 23-S RNA from E. coli. Three main ribonucleoproteins were identified. The largest was only obtained in an impure state at low [T1] RNase concentrations, but the 2 smaller ones, which were difficult to separate from one another electrophoretically, were stable over a range of enzyme concentrations. The 2 smaller ribonucleoproteins yielded a total of 13 RNA subfragments that were judged to be homogeneous electrophoretically. The latter were characterized for molecular weight and the subfragment composition of each of these ribonucleoproteins was established. The subfragments were maintained together in each ribonucleoprotein by RNA-RNA interactions. The primary and specific binding site of protein L1 was localized on 1 continuous RNA subfragment of .apprx. 110 nucleotides in length by 2 newly developed binding methods.