Dynamics of uS19 C-Terminal Tail during the Translation Elongation Cycle in Human Ribosomes.
ribosome
single-particle cryo-EM
translational accuracy
uS19 protein
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
07 04 2020
07 04 2020
Historique:
received:
21
06
2019
revised:
06
12
2019
accepted:
12
03
2020
entrez:
9
4
2020
pubmed:
9
4
2020
medline:
28
4
2021
Statut:
ppublish
Résumé
Ribosomes undergo multiple conformational transitions during translation elongation. Here, we report the high-resolution cryoelectron microscopy (cryo-EM) structure of the human 80S ribosome in the post-decoding pre-translocation state (classical-PRE) at 3.3-Å resolution along with the rotated (hybrid-PRE) and the post-translocation states (POST). The classical-PRE state ribosome structure reveals a previously unobserved interaction between the C-terminal region of the conserved ribosomal protein uS19 and the A- and P-site tRNAs and the mRNA in the decoding site. In addition to changes in the inter-subunit bridges, analysis of different ribosomal conformations reveals the dynamic nature of this domain and suggests a role in tRNA accommodation and translocation during elongation. Furthermore, we show that disease-associated mutations in uS19 result in increased frameshifting. Together, this structure-function analysis provides mechanistic insights into the role of the uS19 C-terminal tail in the context of mammalian ribosomes.
Identifiants
pubmed: 32268098
pii: S2211-1247(20)30351-X
doi: 10.1016/j.celrep.2020.03.037
pii:
doi:
Substances chimiques
RNA, Messenger
0
Ribosomal Proteins
0
ribosomal protein S19
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
107473Informations de copyright
Copyright © 2020 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of Interests The authors declare no competing interests.