Oct 29, 2018

The CryoEM Structure of the Ribosome Maturation Factor Rea1

BioRxiv : the Preprint Server for Biology
Piotr SosnowskiHelgo Schmidt

Abstract

The biogenesis of the 60S ribosomal subunit 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 visualize 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 of Rea1 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.

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Mentioned in this Paper

FEN1
Adenosine Triphosphatases
Ribosome Subunits, Large, Eukaryotic
MDN1 protein, S cerevisiae
Biologic Development
Cell Nucleus
Ribosomal RNA
Docking -molecular Interaction
Site
GOLPH3 gene

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