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dc.contributor.authorKaczmarek Michaels, Katarzyna
dc.contributor.authorMohd Mostafa, Salwa
dc.contributor.authorRuiz Capella, Julia
dc.contributor.authorMoore, Claire L.
dc.date.accessioned2021-10-28T08:54:32Z
dc.date.available2021-10-28T08:54:32Z
dc.date.issued2020
dc.identifier.issn0305-1048spa
dc.identifier.urihttp://hdl.handle.net/10641/2532
dc.description.abstractAdjusting DNA structure via epigenetic modifications, and altering polyadenylation (pA) sites at which precursor mRNA is cleaved and polyadenylated, allows cells to quickly respond to environmental stress. Since polyadenylation occurs cotranscriptionally, and specific patterns of nucleosome positioning and chromatin modifications correlate with pA site usage, epigenetic factors potentially affect alternative polyadenylation (APA). We report that the histone H3K4 methyltransferase Set1, and the histone H3K36 methyltransferase Set2, control choice of pA site in Saccharomyces cerevisiae, a powerful model for studying evolutionarily conserved eukaryotic processes. Deletion of SET1 or SET2 causes an increase in serine-2 phosphorylation within the C-terminal domain of RNA polymerase II (RNAP II) and in the recruitment of the cleavage/polyadenylation complex, both of which could cause the observed switch in pA site usage. Chemical inhibition of TOR signaling, which causes nutritional stress, results in Set1- and Set2- dependent APA. In addition, Set1 and Set2 decrease efficiency of using single pA sites, and control nucleosome occupancy around pA sites. Overall, our study suggests that the methyltransferases Set1 and Set2 regulate APA induced by nutritional stress, affect the RNAP II C-terminal domain phosphorylation at Ser2, and control recruitment of the 3 end processing machinery to the vicinity of pA sites.spa
dc.language.isoengspa
dc.publisherNucleic Acids Researchspa
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.titleRegulation of alternative polyadenylation in the yeast Saccharomyces cerevisiae by histone H3K4 and H3K36 methyltransferases.spa
dc.typearticlespa
dc.description.versionpost-printspa
dc.rights.accessRightsopenAccessspa
dc.description.extent1.432 KBspa
dc.identifier.doi10.1093/nar/gkaa292spa
dc.relation.publisherversionhttps://academic.oup.com/nar/article/48/10/5407/5827662spa


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Except where otherwise noted, this item's license is described as Atribución-NoComercial-SinDerivadas 3.0 España