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Mechanisms that ensure speed and fidelity in eukaryotic translation termination.


ABSTRACT: 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.

SUBMITTER: Lawson MR 

PROVIDER: S-EPMC9017434 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature

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Mechanisms that ensure speed and fidelity in eukaryotic translation termination.

Lawson Michael R MR   Lessen Laura N LN   Wang Jinfan J   Prabhakar Arjun A   Corsepius Nicholas C NC   Green Rachel R   Puglisi Joseph D JD  

Science (New York, N.Y.) 20210801 6557


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  ...[more]

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