Translation Termination Factor eRF3 Mediates mRNA Decay through the Regulation of Deadenylation *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 278, Issue: 40, Page: 38287-38291
2003
- 136Citations
- 124Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations136
- Citation Indexes136
- 136
- CrossRef120
- Captures124
- Readers124
- 124
Article Description
Messenger RNA decay, which is a regulated process intimately linked to translation, begins with the deadenylation of the poly(A) tail at the 3′ end. However, the precise mechanism triggering the first step of mRNA decay and its relationship to translation have not been elucidated. Here, we show that the translation termination factor eRF3 mediates mRNA deadenylation and decay in the yeast Saccharomyces cerevisiae. The N-domain of eRF3, which is not necessarily required for translation termination, interacts with the poly(A)-binding protein PABP. When this interaction is blocked by means of deletion or overexpression of the N-domain of eRF3, half-lives of all mRNAs are prolonged. The eRF3 mutant lacking the N-domain is deficient in the poly(A) shortening. Furthermore, the eRF3-mediated mRNA decay requires translation to proceed, especially ribosomal transition through the termination codon. These results indicate that the N-domain of eRF3 mediates mRNA decay by regulating deadenylation in a manner coupled to translation.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925820831305; http://dx.doi.org/10.1074/jbc.c300300200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0141866883&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12923185; http://www.jbc.org/lookup/doi/10.1074/jbc.C300300200; https://syndication.highwire.org/content/doi/10.1074/jbc.C300300200; https://linkinghub.elsevier.com/retrieve/pii/S0021925820831305; https://dx.doi.org/10.1074/jbc.c300300200
American Society for Biochemistry & Molecular Biology (ASBMB)
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