Dissecting macromolecular recognition sites in ribosome: implication to its self-assembly.

ABSTRACT: Interactions between macromolecules play a crucial role in ribosome assembly that follows a highly coordinated process involving RNA folding and binding of ribosomal proteins (r-proteins). Although extensive studies have been carried out to understand macromolecular interactions in ribosomes, most of them are confined to either large or small ribosomal-subunit of few species. A comparative analysis of macromolecular interactions across different domains is still missing. We have analyzed the structural and physicochemical properties of protein-protein (PP), protein-RNA (PR) and RNA-RNA (RR) interfaces in small and large subunits of ribosomes, as well as in between the two subunits. Additionally, we have also developed Random Forest (RF) classifier to catalog the r-proteins. We find signifi

SUBMITTER: Pilla SP 

PROVIDER: S-EPMC6693545 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature