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TitleHelicase-mediated mechanism of SSU processome maturation and disassembly.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateOct 29, 2025
AuthorsOlga Buzovetsky / Sebastian Klinge
PubMed AbstractEukaryotic ribosomal small subunit (SSU) assembly requires the SSU processome, a nucleolar precursor containing the RNA chaperone U3 snoRNA. The underlying molecular mechanisms of SSU processome ...Eukaryotic ribosomal small subunit (SSU) assembly requires the SSU processome, a nucleolar precursor containing the RNA chaperone U3 snoRNA. The underlying molecular mechanisms of SSU processome maturation, remodeling, disassembly, RNA quality control, and the transitions between states remain elusive due to a paucity of intermediates . Here we report 16 native SSU processome structures alongside genetic data, revealing how two helicases, the Mtr4-exosome and Dhr1, are controlled for accurate and unidirectional ribosome biogenesis. Our data show how irreversible pre-ribosomal RNA degradation by the redundantly tethered RNA exosome couples the transformation of the SSU processome into a pre-40 particle during which Utp14 can probe evolving surfaces, ultimately positioning and activating Dhr1 to unwind the U3 snoRNA and initiate nucleolar pre-40 release. This study highlights a paradigm for large dynamic RNA-protein complexes where irreversible RNA degradation drives compositional changes and communicates these changes to govern enzyme activity while maintaining overall quality control.
External linksbioRxiv / PubMed:41256391 / PubMed Central
MethodsEM (single particle)
Resolution3.32 Å
Structure data

EMDB-48937: SSU processome maturation and disassembly, State A - UtpC focused map
Method: EM (single particle) / Resolution: 3.32 Å

Source
  • Saccharomyces cerevisiae BY4741 (yeast)

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