A Conserved Ribosomal Protein Has Entirely Dissimilar Structures in Different Organisms.

ABSTRACT: Ribosomes from different species can markedly differ in their composition by including dozens of ribosomal proteins that are unique to specific lineages but absent in others. However, it remains unknown how ribosomes acquire new proteins throughout evolution. Here, to help answer this question, we describe the evolution of the ribosomal protein msL1/msL2 that was recently found in ribosomes from the parasitic microorganism clade, microsporidia. We show that this protein has a conserved location in the ribosome but entirely dissimilar structures in different organisms: in each of the analyzed species, msL1/msL2 exhibits an altered secondary structure, an inverted orientation of the N-termini and C-termini on the ribosomal binding surface, and a completely transformed 3D fold. We then show t

SUBMITTER: Schierholz L 

PROVIDER: S-EPMC10764239 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature