Sequence Analysis and Comparative Study of the Protein Subunits of Archaeal RNase P

摘要: RNase P, a ribozyme-based ribonucleoprotein (RNP) complex that catalyzes tRNA 5′-maturation, is ubiquitous in all domains of life, but the evolution its protein components (RNase P proteins, RPPs) not well understood. Archaeal RPPs may provide clues on how evolved from an ancient ribozyme to RNP with multiple archaeal and eukaryotic (homologous) RPPs, which are unrelated single bacterial RPP. Here, we analyzed sequence structure over 600 available genomes. All five found eight phyla, suggesting these arose early evolutionary history. The putative ancestral genomic loci include genes encoding several members ribosome, exosome, proteasome complexes, indicate coevolution/coordinate regulation other core cellular machineries. Despite being ancient, generally lack conservation compared universal proteins. By analyzing relative frequency residues at every position context high-resolution structures each (either alone or as functional binary complexes), suggest for mutational analysis help uncover structure-function relationships RPPs.