Concerted structural rearrangements enable RNA channeling into the cytoplasmic Ski238-Ski7-exosome assembly.


Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
16 Nov 2023
Historique:
received: 06 06 2023
revised: 25 08 2023
accepted: 29 09 2023
medline: 20 11 2023
pubmed: 26 10 2023
entrez: 25 10 2023
Statut: ppublish

Résumé

The Ski2-Ski3-Ski8 (Ski238) helicase complex directs cytoplasmic mRNAs toward the nucleolytic exosome complex for degradation. In yeast, the interaction between Ski238 and exosome requires the adaptor protein Ski7. We determined different cryo-EM structures of the Ski238 complex depicting the transition from a rigid autoinhibited closed conformation to a flexible active open conformation in which the Ski2 helicase module has detached from the rest of Ski238. The open conformation favors the interaction of the Ski3 subunit with exosome-bound Ski7, leading to the recruitment of the exosome. In the Ski238-Ski7-exosome holocomplex, the Ski2 helicase module binds the exosome cap, enabling the RNA to traverse from the helicase through the internal exosome channel to the Rrp44 exoribonuclease. Our study pinpoints how conformational changes within the Ski238 complex regulate exosome recruitment for RNA degradation. We also reveal the remarkable conservation of helicase-exosome RNA channeling mechanisms throughout eukaryotic nuclear and cytoplasmic exosome complexes.

Identifiants

pubmed: 37879335
pii: S1097-2765(23)00803-1
doi: 10.1016/j.molcel.2023.09.037
pmc: PMC10659929
pii:
doi:

Substances chimiques

RNA 63231-63-0
Saccharomyces cerevisiae Proteins 0
Exosome Multienzyme Ribonuclease Complex EC 3.1.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

4093-4105.e7

Informations de copyright

Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests E.C. is a member of the Molecular Cell advisory board.

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Auteurs

Achim Keidel (A)

Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, 82152 Munich, Germany.

Alexander Kögel (A)

Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, 82152 Munich, Germany.

Peter Reichelt (P)

Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, 82152 Munich, Germany.

Eva Kowalinski (E)

EMBL Grenoble, 71 Avenue des Martyrs, 38072 Grenoble, France.

Ingmar B Schäfer (IB)

Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, 82152 Munich, Germany.

Elena Conti (E)

Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, Martinsried, 82152 Munich, Germany. Electronic address: conti@biochem.mpg.de.

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Classifications MeSH