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Title | The CryoEM structure of the ribosome maturation factor Rea1. |
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Journal, issue, pages | Elife, Vol. 7, Year 2018 |
Publish date | Nov 26, 2018 |
Authors | Piotr Sosnowski / Linas Urnavicius / Andreas Boland / Robert Fagiewicz / Johan Busselez / Gabor Papai / Helgo Schmidt / |
PubMed Abstract | 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 ...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. |
External links | Elife / PubMed:30460895 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.9 - 7.8 Å |
Structure data | EMDB-0308, PDB-6hyd: EMDB-0309, PDB-6hyp: EMDB-0329, PDB-6i27: EMDB-0330: |
Chemicals | ChemComp-ADP: |
Source |
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Keywords | MOTOR PROTEIN / Rea1 / Mdn1 / Midasin / AAA+ protein / ribosome maturation / molecular machine |