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dc.contributor.authorGanesan, Robin
dc.contributor.authorMangkalaphiban, Kotchaphorn
dc.contributor.authorBaker, Richard E
dc.contributor.authorHe, Feng
dc.contributor.authorJacobson, Allan
dc.date.accessioned2023-03-03T16:25:12Z
dc.date.available2023-03-03T16:25:12Z
dc.date.issued2022-10-03
dc.identifier.citationGanesan R, Mangkalaphiban K, Baker RE, He F, Jacobson A. Ribosome-bound Upf1 forms distinct 80S complexes and conducts mRNA surveillance. RNA. 2022 Dec;28(12):1621-1642. doi: 10.1261/rna.079416.122. Epub 2022 Oct 3. PMID: 36192133; PMCID: PMC9670811.en_US
dc.identifier.eissn1469-9001
dc.identifier.doi10.1261/rna.079416.122en_US
dc.identifier.pmid36192133
dc.identifier.urihttp://hdl.handle.net/20.500.14038/51744
dc.description.abstractUpf1, Upf2, and Upf3, the central regulators of nonsense-mediated mRNA decay (NMD), appear to exercise their NMD functions while bound to elongating ribosomes, and evidence for this conclusion is particularly compelling for Upf1. Hence, we used selective profiling of yeast Upf1:ribosome association to define that step in greater detail, understand whether the nature of the mRNA being translated influences Upf1:80S interaction, and elucidate the functions of ribosome-associated Upf1. Our approach has allowed us to clarify the timing and specificity of Upf1 association with translating ribosomes, obtain evidence for a Upf1 mRNA surveillance function that precedes the activation of NMD, identify a unique ribosome state that generates 37-43 nt ribosome footprints whose accumulation is dependent on Upf1's ATPase activity, and demonstrate that a mutated form of Upf1 can interfere with normal translation termination and ribosome release. In addition, our results strongly support the existence of at least two distinct functional Upf1 complexes in the NMD pathway.en_US
dc.language.isoenen_US
dc.relation.ispartofRNAen_US
dc.relation.urlhttps://doi.org/10.1261/rna.079416.122en_US
dc.rights© 2022 Ganesan et al. This article, published in RNA, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/ by-nc/4.0/.; Attribution-NonCommercial 4.0 Internationalen_US
dc.rights.urihttp://creativecommons.org/licenses/by-nc/4.0/*
dc.subjectNMD substratesen_US
dc.subjectUpf proteinsen_US
dc.subjectselective ribosome profilingen_US
dc.titleRibosome-bound Upf1 forms distinct 80S complexes and conducts mRNA surveillanceen_US
dc.typeJournal Articleen_US
dc.source.journaltitleRNA (New York, N.Y.)
dc.source.volume28
dc.source.issue12
dc.source.beginpage1621
dc.source.endpage1642
dc.source.countryUnited States
dc.source.countryUnited States
dc.identifier.journalRNA (New York, N.Y.)
refterms.dateFOA2023-03-03T16:25:13Z
dc.contributor.departmentMicrobiology and Physiological Systemsen_US
dc.contributor.departmentMorningside Graduate School of Biomedical Sciencesen_US


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© 2022 Ganesan et al. This article, published in RNA, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/ by-nc/4.0/.; Attribution-NonCommercial 4.0 International
Except where otherwise noted, this item's license is described as © 2022 Ganesan et al. This article, published in RNA, is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/ by-nc/4.0/.; Attribution-NonCommercial 4.0 International