Regulation of alternative polyadenylation in the yeast Saccharomyces cerevisiae by histone H3K4 and H3K36 methyltransferases.
Identifieur interne : 000058 ( Main/Exploration ); précédent : 000057; suivant : 000059Regulation of alternative polyadenylation in the yeast Saccharomyces cerevisiae by histone H3K4 and H3K36 methyltransferases.
Auteurs : Katarzyna Kaczmarek Michaels [États-Unis] ; Salwa Mohd Mostafa [États-Unis] ; Julia Ruiz Capella [Espagne] ; Claire L. Moore [États-Unis]Source :
- Nucleic acids research [ 1362-4962 ] ; 2020.
Descripteurs français
- KwdFr :
- Chromatine (composition chimique), Chromatine (effets des médicaments et des substances chimiques), Délétion de gène (MeSH), Facteurs de clivage et de polyadénylation de l'ARN messager (métabolisme), Histone (MeSH), Histone-lysine N-methyltransferase (génétique), Histone-lysine N-methyltransferase (physiologie), Methyltransferases (génétique), Methyltransferases (physiologie), Nucléosomes (métabolisme), Polyadénylation (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (physiologie), RNA polymerase II (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie).
- MESH :
- composition chimique : Chromatine.
- effets des médicaments et des substances chimiques : Chromatine, Saccharomyces cerevisiae.
- génétique : Histone-lysine N-methyltransferase, Methyltransferases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Facteurs de clivage et de polyadénylation de l'ARN messager, Nucléosomes, RNA polymerase II, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- physiologie : Histone-lysine N-methyltransferase, Methyltransferases, Protéines de Saccharomyces cerevisiae.
- Délétion de gène, Histone, Polyadénylation, Régulation de l'expression des gènes fongiques.
English descriptors
- KwdEn :
- Chromatin (chemistry), Chromatin (drug effects), Gene Deletion (MeSH), Gene Expression Regulation, Fungal (MeSH), Histone-Lysine N-Methyltransferase (genetics), Histone-Lysine N-Methyltransferase (physiology), Histones (MeSH), Methyltransferases (genetics), Methyltransferases (physiology), Nucleosomes (metabolism), Polyadenylation (MeSH), RNA Polymerase II (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (physiology), Sirolimus (pharmacology), mRNA Cleavage and Polyadenylation Factors (metabolism).
- MESH :
- chemical , chemistry : Chromatin.
- chemical , drug effects : Chromatin.
- chemical , genetics : Histone-Lysine N-Methyltransferase, Methyltransferases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Nucleosomes, RNA Polymerase II, mRNA Cleavage and Polyadenylation Factors.
- chemical , pharmacology : Sirolimus.
- chemical , physiology : Histone-Lysine N-Methyltransferase, Methyltransferases, Saccharomyces cerevisiae Proteins.
- drug effects : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Gene Deletion, Gene Expression Regulation, Fungal, Histones, Polyadenylation.
Abstract
Adjusting 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 co-transcriptionally, 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.
DOI: 10.1093/nar/gkaa292
PubMed: 32356874
PubMed Central: PMC7261179
Affiliations:
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Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatine (composition chimique)</term><term>Chromatine (effets des médicaments et des substances chimiques)</term><term>Délétion de gène (MeSH)</term><term>Facteurs de clivage et de polyadénylation de l'ARN messager (métabolisme)</term><term>Histone (MeSH)</term><term>Histone-lysine N-methyltransferase (génétique)</term><term>Histone-lysine N-methyltransferase (physiologie)</term><term>Methyltransferases (génétique)</term><term>Methyltransferases (physiologie)</term><term>Nucléosomes (métabolisme)</term><term>Polyadénylation (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (physiologie)</term><term>RNA polymerase II (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae 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N-Methyltransferase</term><term>Methyltransferases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Chromatine</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Chromatine</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Histone-lysine N-methyltransferase</term><term>Methyltransferases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de clivage et de polyadénylation de l'ARN messager</term><term>Nucléosomes</term><term>RNA polymerase II</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Histone-lysine N-methyltransferase</term><term>Methyltransferases</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Deletion</term><term>Gene Expression Regulation, Fungal</term><term>Histones</term><term>Polyadenylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Délétion de gène</term><term>Histone</term><term>Polyadénylation</term><term>Régulation de l'expression des gènes fongiques</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Adjusting 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 co-transcriptionally, 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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32356874</PMID><DateCompleted><Year>2020</Year><Month>08</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>08</Month><Day>17</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1362-4962</ISSN><JournalIssue CitedMedium="Internet"><Volume>48</Volume><Issue>10</Issue><PubDate><Year>2020</Year><Month>06</Month><Day>04</Day></PubDate></JournalIssue><Title>Nucleic acids research</Title><ISOAbbreviation>Nucleic Acids Res</ISOAbbreviation></Journal><ArticleTitle>Regulation of alternative polyadenylation in the yeast Saccharomyces cerevisiae by histone H3K4 and H3K36 methyltransferases.</ArticleTitle><Pagination><MedlinePgn>5407-5425</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/nar/gkaa292</ELocationID><Abstract><AbstractText>Adjusting 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 co-transcriptionally, 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.</AbstractText><CopyrightInformation>© The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kaczmarek Michaels</LastName><ForeName>Katarzyna</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mohd Mostafa</LastName><ForeName>Salwa</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Tufts University Graduate School of Biomedical Sciences, Boston, MA 02111, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruiz Capella</LastName><ForeName>Julia</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Faculty of Experimental Sciences, Universidad Francisco de Vitoria, Madrid 28223, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Moore</LastName><ForeName>Claire L</ForeName><Initials>CL</Initials><AffiliationInfo><Affiliation>Department of Developmental, Molecular, and Chemical Biology, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Tufts University Graduate School of Biomedical Sciences, Boston, MA 02111, USA.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nucleic Acids Res</MedlineTA><NlmUniqueID>0411011</NlmUniqueID><ISSNLinking>0305-1048</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002843">Chromatin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006657">Histones</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009707">Nucleosomes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D039221">mRNA Cleavage and Polyadenylation Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="C448996">Set2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.43</RegistryNumber><NameOfSubstance UI="D011495">Histone-Lysine N-Methyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.43</RegistryNumber><NameOfSubstance UI="C411250">SET1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.-</RegistryNumber><NameOfSubstance UI="D012319">RNA Polymerase II</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002843" MajorTopicYN="N">Chromatin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017353" MajorTopicYN="N">Gene Deletion</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011495" MajorTopicYN="N">Histone-Lysine N-Methyltransferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006657" MajorTopicYN="N">Histones</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009707" MajorTopicYN="N">Nucleosomes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D026723" MajorTopicYN="Y">Polyadenylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012319" MajorTopicYN="N">RNA Polymerase II</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020123" 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Madrid</li><li>Massachusetts</li></region></list><tree><country name="États-Unis"><noRegion><name sortKey="Kaczmarek Michaels, Katarzyna" sort="Kaczmarek Michaels, Katarzyna" uniqKey="Kaczmarek Michaels K" first="Katarzyna" last="Kaczmarek Michaels">Katarzyna Kaczmarek Michaels</name></noRegion><name sortKey="Mohd Mostafa, Salwa" sort="Mohd Mostafa, Salwa" uniqKey="Mohd Mostafa S" first="Salwa" last="Mohd Mostafa">Salwa Mohd Mostafa</name><name sortKey="Mohd Mostafa, Salwa" sort="Mohd Mostafa, Salwa" uniqKey="Mohd Mostafa S" first="Salwa" last="Mohd Mostafa">Salwa Mohd Mostafa</name><name sortKey="Moore, Claire L" sort="Moore, Claire L" uniqKey="Moore C" first="Claire L" last="Moore">Claire L. Moore</name><name sortKey="Moore, Claire L" sort="Moore, Claire L" uniqKey="Moore C" first="Claire L" last="Moore">Claire L. Moore</name></country><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Ruiz Capella, Julia" sort="Ruiz Capella, Julia" uniqKey="Ruiz Capella J" first="Julia" last="Ruiz Capella">Julia Ruiz Capella</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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