The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1
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 ass...
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eLife Sciences Publications Ltd
2018-11-01
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Online Access: | https://elifesciences.org/articles/39163 |
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author | Piotr Sosnowski Linas Urnavicius Andreas Boland Robert Fagiewicz Johan Busselez Gabor Papai Helgo Schmidt |
author_facet | Piotr Sosnowski Linas Urnavicius Andreas Boland Robert Fagiewicz Johan Busselez Gabor Papai Helgo Schmidt |
author_sort | Piotr Sosnowski |
collection | DOAJ |
description | 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. |
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language | English |
last_indexed | 2024-04-11T09:14:23Z |
publishDate | 2018-11-01 |
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spelling | doaj.art-e61263d14ec247218a0ab7068090309c2022-12-22T04:32:25ZengeLife Sciences Publications LtdeLife2050-084X2018-11-01710.7554/eLife.39163The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1Piotr Sosnowski0https://orcid.org/0000-0003-4902-9560Linas Urnavicius1Andreas Boland2https://orcid.org/0000-0003-1218-6714Robert Fagiewicz3Johan Busselez4https://orcid.org/0000-0002-4078-1265Gabor Papai5Helgo Schmidt6https://orcid.org/0000-0002-8004-8316Institut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, Illkirch, France; Université de Strasbourg, Illkirch, FranceDivision of Structural Studies, MRC Laboratory of Molecular Biology, Cambridge, United KingdomDivision of Structural Studies, MRC Laboratory of Molecular Biology, Cambridge, United KingdomInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, Illkirch, France; Université de Strasbourg, Illkirch, FranceInstitut de Génétique et de Biologie Moléculaire et Cellulaire, Illkirch, France; Centre National de la Recherche Scientifique, UMR7104, Illkirch, France; Institut National de la Santé et de la Recherche Médicale, U964, Illkirch, France; Université de Strasbourg, Illkirch, FranceThe 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.https://elifesciences.org/articles/39163Rea1midasinCryoEMribosome maturationAAA+ proteinmolecular machine |
spellingShingle | Piotr Sosnowski Linas Urnavicius Andreas Boland Robert Fagiewicz Johan Busselez Gabor Papai Helgo Schmidt The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1 eLife Rea1 midasin CryoEM ribosome maturation AAA+ protein molecular machine |
title | The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1 |
title_full | The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1 |
title_fullStr | The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1 |
title_full_unstemmed | The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1 |
title_short | The CryoEM structure of the Saccharomyces cerevisiae ribosome maturation factor Rea1 |
title_sort | cryoem structure of the saccharomyces cerevisiae ribosome maturation factor rea1 |
topic | Rea1 midasin CryoEM ribosome maturation AAA+ protein molecular machine |
url | https://elifesciences.org/articles/39163 |
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