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.

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