Ancestral Interactions of Ribosomal RNA and Ribosomal Proteins.

ABSTRACT: We have proposed that the ancient ribosome increased in size during early evolution by addition of small folding-competent RNAs. In this Accretion Model, small RNAs and peptides were subsumed onto subunit surfaces, gradually encasing and freezing previously acquired components. The model predicts that appropriate rRNA fragments have inherited local autonomy of folding and local autonomy of assembly with ribosomal proteins (rProteins), and that the rProtein and rRNA are co-chaperones. To test these predictions, we investigate the rRNA interactions of rProtein uL23 and its tail, uL23^tail, which is a β-hairpin that penetrates deep into the core of the large ribosomal subunit. In the assembled ribosome, uL23^tail associates with Domain III of the rRNA and a subdomain calle

SUBMITTER: Lanier KA 

PROVIDER: S-EPMC5529175 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature