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Article Dans Une Revue Molecular Cell Année : 2020

Structures of B. subtilis Maturation RNases Captured on 50S Ribosome with Pre-rRNAs

Résumé

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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Dates et versions

hal-03015124 , version 1 (19-11-2020)

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Stephanie Oerum, Tom Dendooven, Marjorie Catala, Laetitia Gilet, Clément Dégut, et al.. Structures of B. subtilis Maturation RNases Captured on 50S Ribosome with Pre-rRNAs. Molecular Cell, 2020, 80 (2), pp.227-236.e5. ⟨10.1016/j.molcel.2020.09.008⟩. ⟨hal-03015124⟩
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