Molecular paleontology: a biochemical model of the ancestral ribosome.

TitleMolecular paleontology: a biochemical model of the ancestral ribosome.
Publication TypeJournal Article
Year of Publication2013
AuthorsHsiao, C, Lenz, TK, Peters, JK, Fang, P-Y, Schneider, DM, Anderson, EJ, Preeprem, T, Bowman, JC, O'Neill, EB, Lie, L, Athavale, SS, J Gossett, J, Trippe, C, Murray, J, Petrov, AS, Wartell, RM, Harvey, SC, Hud, NV, Williams, LDean
JournalNucleic Acids Res
Date Published2013 Mar 1
KeywordsEvolution, Molecular, Magnesium, Models, Genetic, Models, Molecular, Nucleic Acid Conformation, Peptide Fragments, Protein Binding, Ribonuclease H, Ribosomal Proteins, Ribosomes, RNA Cleavage, RNA, Bacterial, RNA, Ribosomal, 23S, Thermus thermophilus

Ancient components of the ribosome, inferred from a consensus of previous work, were constructed in silico, in vitro and in vivo. The resulting model of the ancestral ribosome presented here incorporates ∼20% of the extant 23S rRNA and fragments of five ribosomal proteins. We test hypotheses that ancestral rRNA can: (i) assume canonical 23S rRNA-like secondary structure, (ii) assume canonical tertiary structure and (iii) form native complexes with ribosomal protein fragments. Footprinting experiments support formation of predicted secondary and tertiary structure. Gel shift, spectroscopic and yeast three-hybrid assays show specific interactions between ancestral rRNA and ribosomal protein fragments, independent of other, more recent, components of the ribosome. This robustness suggests that the catalytic core of the ribosome is an ancient construct that has survived billions of years of evolution without major changes in structure. Collectively, the data here support a model in which ancestors of the large and small subunits originated and evolved independently of each other, with autonomous functionalities.

Alternate JournalNucleic Acids Res.
PubMed ID23355613
PubMed Central IDPMC3597689