Summary information and primary citation
- PDB-id
- 6tpq; SNAP-derived features in text and JSON formats;
DNAproDB
- Class
- ribosomal protein
- Method
- cryo-EM (3.07 Å)
- Summary
- Rnase m5 bound to 50s ribosome with precursor 5s rrna
- Reference
- Oerum S, Dendooven T, Catala M, Gilet L, Degut C, Trinquier A, Bourguet M, Barraud P, Cianferani S, Luisi BF, Condon C, Tisne C (2020): "Structures of B. subtilis Maturation RNases Captured on 50S Ribosome with Pre-rRNAs." Mol.Cell, 80, 227. doi: 10.1016/j.molcel.2020.09.008.
- Abstract
- The pathways for ribosomal RNA (rRNA) maturation diverge greatly among the domains of life. In the Gram-positive model bacterium, Bacillus subtilis, the final maturation steps of the two large ribosomal subunit (50S) rRNAs, 23S and 5S pre-rRNAs, are catalyzed by the double-strand specific ribonucleases (RNases) Mini-RNase III and RNase M5, respectively. Here we present a protocol that allowed us to solve the 3.0 and 3.1 Å resolution cryoelectron microscopy structures of these RNases poised to cleave their pre-rRNA substrates within the B. subtilis 50S particle. These data provide the first structural insights into rRNA maturation in bacteria by revealing how these RNases recognize and process double-stranded pre-rRNA. Our structures further uncover how specific ribosomal proteins act as chaperones to correctly fold the pre-rRNA substrates and, for Mini-III, anchor the RNase to the ribosome. These r-proteins thereby serve a quality-control function in the process from accurate ribosome assembly to rRNA processing.