Journal
SCIENCE
Volume 373, Issue 6557, Pages 876-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abi7801
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Funding
- A.P. Giannini Foundation
- Cystic Fibrosis Foundation [PUGLISI20GO]
- National Institute of General Medical Sciences [R37GM059425, R01GM113078, R01GM51266]
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Through single-molecule fluorescence assays, researchers found that in the termination process of yeast translation, the two release factors eRF1 and eRF3 bind together to rapidly recognize stop codons and induce termination through a tightly regulated, multistep process that resembles transfer RNA selection during translation elongation.
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.
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