Summary information and primary citation
- PDB-id
-
6tpq;
SNAP-derived features in text and
JSON formats
- 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.
