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TitleConcurrent remodelling of nucleolar 60S subunit precursors by the Rea1 ATPase and Spb4 RNA helicase.
Journal, issue, pagesElife, Vol. 12, Year 2023
Publish dateMar 17, 2023
AuthorsValentin Mitterer / Matthias Thoms / Robert Buschauer / Otto Berninghausen / Ed Hurt / Roland Beckmann /
PubMed AbstractBiogenesis intermediates of nucleolar ribosomal 60S precursor particles undergo a number of structural maturation steps before they transit to the nucleoplasm and are finally exported into the ...Biogenesis intermediates of nucleolar ribosomal 60S precursor particles undergo a number of structural maturation steps before they transit to the nucleoplasm and are finally exported into the cytoplasm. The AAA-ATPase Rea1 participates in the nucleolar exit by releasing the Ytm1-Erb1 heterodimer from the evolving pre-60S particle. Here, we show that the DEAD-box RNA helicase Spb4 with its interacting partner Rrp17 is further integrated into this maturation event. Spb4 binds to a specific class of late nucleolar pre-60S intermediates, whose cryo-EM structure revealed how its helicase activity facilitates melting and restructuring of 25S rRNA helices H62 and H63/H63a prior to Ytm1-Erb1 release. In vitro maturation of such Spb4-enriched pre-60S particles, incubated with purified Rea1 and its associated pentameric Rix1-complex in the presence of ATP, combined with cryo-EM analysis depicted the details of the Rea1-dependent large-scale pre-ribosomal remodeling. Our structural insights unveil how the Rea1 ATPase and Spb4 helicase remodel late nucleolar pre-60S particles by rRNA restructuring and dismantling of a network of several ribosomal assembly factors.
External linksElife / PubMed:36929751 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

EMDB-16276: Release state - ES27up (pre-60S)
Method: EM (single particle) / Resolution: 3.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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