Sequence-specific remodeling of a topologically complex RNP substrate by Spb4

Victor Emmanuel Cruz, Kamil Sekulski, Nagesh Peddada, Carolin Sailer, Sahana Balasubramanian, Christine S. S. Weirich, Florian Stengel, Jan P. Erzberger*

*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

14 Citationer (Scopus)

Abstract

DEAD-box ATPases are ubiquitous enzymes essential in all aspects of RNA biology. However, the limited in vitro catalytic activities described for these enzymes are at odds with their complex cellular roles, most notably in driving large-scale RNA remodeling steps during the assembly of ribonucleoproteins (RNPs). We describe cryo-EM structures of 60S ribosomal biogenesis intermediates that reveal how context-specific RNA unwinding by the DEAD-box ATPase Spb4 results in extensive, sequence-specific remodeling of rRNA secondary structure. Multiple cis and trans interactions stabilize Spb4 in a post-catalytic, high-energy intermediate that drives the organization of the three-way junction at the base of rRNA domain IV. This mechanism explains how limited strand separation by DEAD-box ATPases is leveraged to provide non-equilibrium directionality and ensure efficient and accurate RNP assembly.

OriginalsprogEngelsk
TidsskriftNature Structural & Molecular Biology
Vol/bind29
Sider (fra-til)1228–1238
Antal sider23
ISSN1545-9993
DOI
StatusE-pub ahead of print - 2022
Udgivet eksterntJa

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