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-Structure paper
Title | A single 2'-O-methylation of ribosomal RNA gates assembly of a functional ribosome. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 30, Issue 1, Page 91-98, Year 2023 |
Publish date | Dec 19, 2022 |
Authors | James N Yelland / Jack P K Bravo / Joshua J Black / David W Taylor / Arlen W Johnson / |
PubMed Abstract | RNA modifications are widespread in biology and abundant in ribosomal RNA. However, the importance of these modifications is not well understood. We show that methylation of a single nucleotide, in ...RNA modifications are widespread in biology and abundant in ribosomal RNA. However, the importance of these modifications is not well understood. We show that methylation of a single nucleotide, in the catalytic center of the large subunit, gates ribosome assembly. Massively parallel mutational scanning of the essential nuclear GTPase Nog2 identified important interactions with rRNA, particularly with the 2'-O-methylated A-site base Gm2922. We found that methylation of G2922 is needed for assembly and efficient nuclear export of the large subunit. Critically, we identified single amino acid changes in Nog2 that completely bypass dependence on G2922 methylation and used cryoelectron microscopy to directly visualize how methylation flips Gm2922 into the active site channel of Nog2. This work demonstrates that a single RNA modification is a critical checkpoint in ribosome biogenesis, suggesting that such modifications can play an important role in regulation and assembly of macromolecular machines. |
External links | Nat Struct Mol Biol / PubMed:36536102 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.9 Å |
Structure data | EMDB-26485, PDB-7ug6: |
Chemicals | ChemComp-GDP: ChemComp-MG: |
Source |
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Keywords | RIBOSOME / ribosome biogenesis / rRNA modification / methylation |