Structural basis of ribosomal 30S subunit degradation by RNase R.

ABSTRACT: Protein synthesis is a major energy-consuming process of the cell that requires the controlled production^1-3 and turnover^4,5 of ribosomes. Although the past few years have seen major advances in our understanding of ribosome biogenesis, structural insight into the degradation of ribosomes has been lacking. Here we present native structures of two distinct small ribosomal 30S subunit degradation intermediates associated with the 3' to 5' exonuclease ribonuclease R (RNase R). The structures reveal that RNase R binds at first to the 30S platform to facilitate the degradation of the functionally important anti-Shine-Dalgarno sequence and the decoding-site helix 44. RNase R then encounters a roadblock when it reaches the neck region of the 30S subunit, and this is overcome

SUBMITTER: Dimitrova-Paternoga L 

PROVIDER: S-EPMC10901742 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature