Scientific article
Open access

The cryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1

Published ineLife, vol. 7, e39163
Publication date2018-11-26
First online date2018-11-26

The biogenesis of 60S ribosomal subunits is initiated in the nucleus where rRNAs and proteins form pre-60S particles. These pre-60S particles mature by transiently interacting with various assembly factors. The ~5000 amino-acid AAA+ ATPase Rea1 (or Midasin) generates force to mechanically remove assembly factors from pre-60S particles, which promotes their export to the cytosol. Here we present three Rea1 cryoEM structures. We visualise the Rea1 engine, a hexameric ring of AAA+ domains, and identify an α-helical bundle of AAA2 as a major ATPase activity regulator. The α-helical bundle interferes with nucleotide-induced conformational changes that create a docking site for the substrate binding MIDAS domain on the AAA +ring. Furthermore, we reveal the architecture of the Rea1 linker, which is involved in force generation and extends from the AAA+ ring. The data presented here provide insights into the mechanism of one of the most complex ribosome maturation factors.

  • AAA+ protein
  • CryoEM
  • Rea1
  • S. cerevisiae
  • Midasin
  • Molecular biophysics
  • Molecular machine
  • Ribosome maturation
  • Structural biology
Affiliation Not a UNIGE publication
  • Medical Research Council - [MC_UP_A025_1011]
  • ATIP-Avenir - [CDP 0B1INSB-HS-9ADO1051]
  • Labex - [ANR-10-LABEX-30-HS]
  • Région Grand Est - [jeunes chercheurs fellowship]
Citation (ISO format)
SOSNOWSKI, Piotr et al. The cryoEM structure of the S<i>accharomyces cerevisiae</i> ribosome maturation factor Rea1. In: eLife, 2018, vol. 7, p. e39163. doi: 10.7554/eLife.39163
Main files (1)
Article (Published version)
ISSN of the journal2050-084X

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