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dc.contributor.authorLee, Susan D.
dc.contributor.authorLiu, Hui-Yun
dc.contributor.authorGraber, Joel H.
dc.contributor.authorHeller-Trulli, Daniel
dc.contributor.authorMichaels, Katarzyna Kaczmarek
dc.contributor.authorCerezo, Juan Francisco
dc.contributor.authorMoore, Claire L.
dc.date.accessioned2021-12-03T07:55:00Z
dc.date.available2021-12-03T07:55:00Z
dc.date.issued2020
dc.identifier.issn1547-6286spa
dc.identifier.urihttp://hdl.handle.net/10641/2612
dc.description.abstractMutation of the essential yeast protein Ipa1 has previously been demonstrated to cause defects in premRNA 3ʹ end processing and growth, but the mechanism underlying these defects was not clear. In this study, we show that the ipa1-1 mutation causes a striking depletion of Ysh1, the evolutionarily conserved endonuclease subunit of the 19-subunit mRNA Cleavage/Polyadenylation (C/P) complex, but does not decrease other C/P subunits. YSH1 overexpression rescues both the growth and 3ʹ end processing defects of the ipa1-1 mutant. YSH1 mRNA level is unchanged in ipa1-1 cells, and proteasome inactivation prevents Ysh1 loss and causes accumulation of ubiquitinated Ysh1. Ysh1 ubiquitination is mediated by the Ubc4 ubiquitin-conjugating enzyme and Mpe1, which in addition to its function in C/P, is also a RING ubiquitin ligase. In summary, Ipa1 affects mRNA processing by controlling the availability of the C/P endonuclease and may represent a regulatory mechanism that could be rapidly deployed to facilitate reprogramming of cellular responses.spa
dc.language.isoengspa
dc.publisherRNA Biologyspa
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.subjectPolyadenylationspa
dc.subjectUbiquitinationspa
dc.subjectAlternative mRNA processingspa
dc.titleRegulation of the Ysh1 endonuclease of the mRNA cleavage/polyadenylation complex by ubiquitinmediated degradation.spa
dc.typejournal articlespa
dc.type.hasVersionAMspa
dc.rights.accessRightsopen accessspa
dc.description.extent4,60 MBspa
dc.identifier.doi10.1080/15476286.2020.1724717spa
dc.relation.publisherversionhttps://www.tandfonline.com/doi/full/10.1080/15476286.2020.1724717spa


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