Structural basis for RNA surveillance by the human nuclear exosome targeting (NEXT) complex.
DExH-box
RNA surveillance
RNA-protein complex
SF2
cryo-EM structure
exosome
helicase
kinase
oncogene
translocase
Journal
Cell
ISSN: 1097-4172
Titre abrégé: Cell
Pays: United States
ID NLM: 0413066
Informations de publication
Date de publication:
09 06 2022
09 06 2022
Historique:
received:
14
10
2021
revised:
04
03
2022
accepted:
08
04
2022
entrez:
10
6
2022
pubmed:
11
6
2022
medline:
15
6
2022
Statut:
ppublish
Résumé
RNA quality control relies on co-factors and adaptors to identify and prepare substrates for degradation by ribonucleases such as the 3' to 5' ribonucleolytic RNA exosome. Here, we determined cryogenic electron microscopy structures of human nuclear exosome targeting (NEXT) complexes bound to RNA that reveal mechanistic insights to substrate recognition and early steps that precede RNA handover to the exosome. The structures illuminate ZCCHC8 as a scaffold, mediating homodimerization while embracing the MTR4 helicase and flexibly anchoring RBM7 to the helicase core. All three subunits collaborate to bind the RNA, with RBM7 and ZCCHC8 surveying sequences upstream of the 3' end to facilitate RNA capture by MTR4. ZCCHC8 obscures MTR4 surfaces important for RNA binding and extrusion as well as MPP6-dependent recruitment and docking onto the RNA exosome core, interactions that contribute to RNA surveillance by coordinating RNA capture, translocation, and extrusion from the helicase to the exosome for decay.
Identifiants
pubmed: 35688134
pii: S0092-8674(22)00463-9
doi: 10.1016/j.cell.2022.04.016
pmc: PMC9210550
mid: NIHMS1799041
pii:
doi:
Substances chimiques
Nuclear Proteins
0
RNA
63231-63-0
Exosome Multienzyme Ribonuclease Complex
EC 3.1.-
DNA Helicases
EC 3.6.4.-
DEAD-box RNA Helicases
EC 3.6.4.13
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2132-2147.e26Subventions
Organisme : Howard Hughes Medical Institute
Pays : United States
Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM118080
Pays : United States
Commentaires et corrections
Type : CommentIn
Informations de copyright
Copyright © 2022 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing financial interests.
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