Mechanisms that ensure speed and fidelity in eukaryotic translation termination.
Codon, Terminator
Fluorescence Resonance Energy Transfer
Peptide Chain Termination, Translational
Peptide Termination Factors
/ metabolism
Protein Binding
Protein Biosynthesis
Ribosomes
/ metabolism
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ metabolism
Single Molecule Imaging
Journal
Science (New York, N.Y.)
ISSN: 1095-9203
Titre abrégé: Science
Pays: United States
ID NLM: 0404511
Informations de publication
Date de publication:
20 08 2021
20 08 2021
Historique:
received:
02
04
2021
accepted:
07
07
2021
entrez:
20
8
2021
pubmed:
21
8
2021
medline:
28
8
2021
Statut:
ppublish
Résumé
Translation termination, which liberates a nascent polypeptide from the ribosome specifically at stop codons, must occur accurately and rapidly. We established single-molecule fluorescence assays to track the dynamics of ribosomes and two requisite release factors (eRF1 and eRF3) throughout termination using an in vitro-reconstituted yeast translation system. We found that the two eukaryotic release factors bound together to recognize stop codons rapidly and elicit termination through a tightly regulated, multistep process that resembles transfer RNA selection during translation elongation. Because the release factors are conserved from yeast to humans, the molecular events that underlie yeast translation termination are likely broadly fundamental to eukaryotic protein synthesis.
Identifiants
pubmed: 34413231
pii: 373/6557/876
doi: 10.1126/science.abi7801
pmc: PMC9017434
mid: NIHMS1795024
doi:
Substances chimiques
Codon, Terminator
0
Peptide Termination Factors
0
SUP45 protein, S cerevisiae
0
Saccharomyces cerevisiae Proteins
0
peptide-chain-release factor 3
0
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
876-882Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM051266
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM113078
Pays : United States
Organisme : NIGMS NIH HHS
ID : R37 GM059425
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008403
Pays : United States
Informations de copyright
Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works.
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