Specific binding of a prokaryotic ribosomal protein to a eukaryotic ribosomal RNA: implications for evolution and autoregulation.

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Abstract
Ribosomal protein L1 from the prokaryote Escherichia coli evidently forms a specific complex with 26S rRNA from the eukaryote Dictyostelium discoideum. The segment of Dictyostelium rRNA protected from ribonuclease digestion by L1 and the corresponding region in Dictyostelium rDNA were investigated by nucleotide sequence analysis and an analogous section in rDNA from Xenopus laevis was identified. When the L1-specific segments from eukaryotic rRNA were compared with those from prokaryotic rRNA, striking similarities in both primary and secondary structure were apparent. A common structural basis for protein recognition is suggested and apparently such regions became fixed at a very early stage in rRNA evolution. Certain structural elements of the L1 binding sites in rRNA are found in the initial segment of the polycistronic L11-L1 mRNA; probably participates in the regulation of ribosomal protein synthesis by specific interaction with its own mRNA.