Shape changes and cooperativity in the folding of the central domain of the 16S ribosomal RNA.

ABSTRACT: Both the small and large subunits of the ribosome, the molecular machine that synthesizes proteins, are complexes of ribosomal RNAs (rRNAs) and a number of proteins. In bacteria, the small subunit has a single 16S rRNA whose folding is the first step in its assembly. The central domain of the 16S rRNA folds independently, driven either by Mg²⁺ ions or by interaction with ribosomal proteins. To provide a quantitative description of ion-induced folding of the ∼350-nucleotide rRNA, we carried out extensive coarse-grained molecular simulations spanning Mg²⁺ concentration between 0 and 30 mM. The Mg²⁺ dependence of the radius of gyration shows that globally the rRNA folds cooperatively. Surprisingly, various structural elements order at different Mg²⁺

SUBMITTER: Hori N 

PROVIDER: S-EPMC7958424 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature