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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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Main Authors: Mitterer, Valentin (Author) , Thoms, Matthias (Author) , Buschauer, Thomas (Author) , Berninghausen, Otto (Author) , Hurt, Ed (Author) , Beckmann, Roland (Author)
Format: Article (Journal)
Language:English
Published: 17 March 2023
In: eLife
Year: 2023, Volume: 12, Pages: 1-22
ISSN:2050-084X
DOI:10.7554/eLife.84877
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.7554/eLife.84877
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Author Notes:Valentin Mitterer, Matthias Thoms, Robert Buschauer, Otto Berninghausen, Ed Hurt, Roland Beckmann

MARC

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520 |a 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. 
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