Abstract
Escherichia coli 5S RNA and its specific protein complexes were hydrolyzed with the single-strand-specific nuclease S1. A tertiary structural model for E. coli 5S RNA is proposed in which ribosomal proteins E-L5, E-L18 and E-L25 influence the conformation of the RNA. This may be of significance for ribosomal function. Comparison of the proposed E. coli 5S RNA structure with those of 18 other prokaryotic 5S RNA led to a generalized eubacterial 5S RNA tertiary structure in which the majority of the conserved nucleotides are in non-base-paired regions and several conserved looped-out adenines (in E. coli, adenines -52, -53, -57, -58 and -66) could be important for protein recognition or interaction or both.