Concurrent remodelling of nucleolar 60S subunit precursors by the Rea1 ATPase and Spb4 RNA helicase

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 f...

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Hauptverfasser: Mitterer, Valentin (VerfasserIn) , Thoms, Matthias (VerfasserIn) , Buschauer, Thomas (VerfasserIn) , Berninghausen, Otto (VerfasserIn) , Hurt, Ed (VerfasserIn) , Beckmann, Roland (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 17 March 2023
In: eLife
Year: 2023, Jahrgang: 12, Pages: 1-22
ISSN:2050-084X
DOI:10.7554/eLife.84877
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.7554/eLife.84877
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Verfasserangaben:Valentin Mitterer, Matthias Thoms, Robert Buschauer, Otto Berninghausen, Ed Hurt, Roland Beckmann
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Zusammenfassung: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.
Beschreibung:Gesehen am 12.06.2023
Beschreibung:Online Resource
ISSN:2050-084X
DOI:10.7554/eLife.84877