RapamycinFungusV1, Main, Exploration, bibRecord, 000726

TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity.

Identifieur interne : 000726 ( Main/Exploration ); précédent : 000725; suivant : 000727

TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity.

Auteurs : Pierre Chymkowitch [Norvège] ; Aurélie Nguéa P [Norvège] ; H Vard Aanes [Norvège] ; Joseph Robertson [Norvège] ; Arne Klungland [Norvège] ; Jorrit M. Enserink [Norvège]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2017.

RBID : pubmed:28096404

Descripteurs français

KwdFr :
- ARN de transfert (biosynthèse), ARN de transfert (génétique), ARN fongique (biosynthèse), ARN fongique (génétique), Azote (métabolisme), Facteurs de transcription (effets des médicaments et des substances chimiques), Facteurs de transcription (métabolisme), Gene Ontology (MeSH), Maturation post-traductionnelle des protéines (MeSH), Protéines de Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Protéines de Saccharomyces cerevisiae (métabolisme), RNA polymerase III (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Sous-unités de protéines (MeSH), Substitution d'acide aminé (MeSH), Sumoylation (MeSH), Transcription génétique (MeSH), Ubiquitin-conjugating enzymes (génétique).
MESH :
- biosynthèse : ARN de transfert, ARN fongique.
- croissance et développement : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- génétique : ARN de transfert, ARN fongique, Ubiquitin-conjugating enzymes.
- métabolisme : Azote, Facteurs de transcription, Protéines de Saccharomyces cerevisiae, RNA polymerase III, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- Gene Ontology, Maturation post-traductionnelle des protéines, Régulation de l'expression des gènes fongiques, Sous-unités de protéines, Substitution d'acide aminé, Sumoylation, Transcription génétique.

English descriptors

KwdEn :
- Amino Acid Substitution (MeSH), Gene Expression Regulation, Fungal (MeSH), Gene Ontology (MeSH), Nitrogen (metabolism), Protein Processing, Post-Translational (MeSH), Protein Subunits (MeSH), RNA Polymerase III (metabolism), RNA, Fungal (biosynthesis), RNA, Fungal (genetics), RNA, Transfer (biosynthesis), RNA, Transfer (genetics), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (drug effects), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Sumoylation (MeSH), Transcription Factors (drug effects), Transcription Factors (metabolism), Transcription, Genetic (MeSH), Ubiquitin-Conjugating Enzymes (genetics).
MESH :
- chemical , biosynthesis : RNA, Fungal, RNA, Transfer.
- chemical , drug effects : Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , genetics : RNA, Fungal, RNA, Transfer, Ubiquitin-Conjugating Enzymes.
- chemical , metabolism : Nitrogen, RNA Polymerase III, Saccharomyces cerevisiae Proteins, Transcription Factors.
- drug effects : Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- chemical , pharmacology : Sirolimus.
- Amino Acid Substitution, Gene Expression Regulation, Fungal, Gene Ontology, Protein Processing, Post-Translational, Protein Subunits, Sumoylation, Transcription, Genetic.

Abstract

Maintaining cellular homeostasis under changing nutrient conditions is essential for the growth and development of all organisms. The mechanisms that maintain homeostasis upon loss of nutrient supply are not well understood. By mapping the SUMO proteome in Saccharomyces cerevisiae, we discovered a specific set of differentially sumoylated proteins mainly involved in transcription. RNA polymerase III (RNAPIII) components, including Rpc53, Rpc82, and Ret1, are particularly prominent nutrient-dependent SUMO targets. Nitrogen starvation, as well as direct inhibition of the master nutrient response regulator target of rapamycin complex 1 (TORC1), results in rapid desumoylation of these proteins, which is reflected by loss of SUMO at tRNA genes. TORC1-dependent sumoylation of Rpc82 in particular is required for robust tRNA transcription. Mechanistically, sumoylation of Rpc82 is important for assembly of the RNAPIII holoenzyme and recruitment of Rpc82 to tRNA genes. In conclusion, our data show that TORC1-dependent sumoylation of Rpc82 bolsters the transcriptional capacity of RNAPIII under optimal growth conditions.

DOI: 10.1073/pnas.1615093114
PubMed: 28096404
PubMed Central: PMC5293095

Affiliations:

Norvège

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution (MeSH)</term>
<term>Gene Expression Regulation, Fungal (MeSH)</term>
<term>Gene Ontology (MeSH)</term>
<term>Nitrogen (metabolism)</term>
<term>Protein Processing, Post-Translational (MeSH)</term>
<term>Protein Subunits (MeSH)</term>
<term>RNA Polymerase III (metabolism)</term>
<term>RNA, Fungal (biosynthesis)</term>
<term>RNA, Fungal (genetics)</term>
<term>RNA, Transfer (biosynthesis)</term>
<term>RNA, Transfer (genetics)</term>
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<term>Saccharomyces cerevisiae (growth & development)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Saccharomyces cerevisiae Proteins (drug effects)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Sirolimus (pharmacology)</term>
<term>Sumoylation (MeSH)</term>
<term>Transcription Factors (drug effects)</term>
<term>Transcription Factors (metabolism)</term>
<term>Transcription, Genetic (MeSH)</term>
<term>Ubiquitin-Conjugating Enzymes (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ARN de transfert (biosynthèse)</term>
<term>ARN de transfert (génétique)</term>
<term>ARN fongique (biosynthèse)</term>
<term>ARN fongique (génétique)</term>
<term>Azote (métabolisme)</term>
<term>Facteurs de transcription (effets des médicaments et des substances chimiques)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Gene Ontology (MeSH)</term>
<term>Maturation post-traductionnelle des protéines (MeSH)</term>
<term>Protéines de Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>RNA polymerase III (métabolisme)</term>
<term>Régulation de l'expression des gènes fongiques (MeSH)</term>
<term>Saccharomyces cerevisiae (croissance et développement)</term>
<term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sirolimus (pharmacologie)</term>
<term>Sous-unités de protéines (MeSH)</term>
<term>Substitution d'acide aminé (MeSH)</term>
<term>Sumoylation (MeSH)</term>
<term>Transcription génétique (MeSH)</term>
<term>Ubiquitin-conjugating enzymes (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>RNA, Fungal</term>
<term>RNA, Transfer</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>RNA, Fungal</term>
<term>RNA, Transfer</term>
<term>Ubiquitin-Conjugating Enzymes</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Nitrogen</term>
<term>RNA Polymerase III</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>ARN de transfert</term>
<term>ARN fongique</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</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>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN de transfert</term>
<term>ARN fongique</term>
<term>Ubiquitin-conjugating enzymes</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Azote</term>
<term>Facteurs de transcription</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>RNA polymerase III</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term>
<term>Gene Expression Regulation, Fungal</term>
<term>Gene Ontology</term>
<term>Protein Processing, Post-Translational</term>
<term>Protein Subunits</term>
<term>Sumoylation</term>
<term>Transcription, Genetic</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Gene Ontology</term>
<term>Maturation post-traductionnelle des protéines</term>
<term>Régulation de l'expression des gènes fongiques</term>
<term>Sous-unités de protéines</term>
<term>Substitution d'acide aminé</term>
<term>Sumoylation</term>
<term>Transcription génétique</term>
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<front><div type="abstract" xml:lang="en">Maintaining cellular homeostasis under changing nutrient conditions is essential for the growth and development of all organisms. The mechanisms that maintain homeostasis upon loss of nutrient supply are not well understood. By mapping the SUMO proteome in Saccharomyces cerevisiae, we discovered a specific set of differentially sumoylated proteins mainly involved in transcription. RNA polymerase III (RNAPIII) components, including Rpc53, Rpc82, and Ret1, are particularly prominent nutrient-dependent SUMO targets. Nitrogen starvation, as well as direct inhibition of the master nutrient response regulator target of rapamycin complex 1 (TORC1), results in rapid desumoylation of these proteins, which is reflected by loss of SUMO at tRNA genes. TORC1-dependent sumoylation of Rpc82 in particular is required for robust tRNA transcription. Mechanistically, sumoylation of Rpc82 is important for assembly of the RNAPIII holoenzyme and recruitment of Rpc82 to tRNA genes. In conclusion, our data show that TORC1-dependent sumoylation of Rpc82 bolsters the transcriptional capacity of RNAPIII under optimal growth conditions.</div>
</front>
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<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28096404</PMID>
<DateCompleted><Year>2018</Year>
<Month>04</Month>
<Day>24</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>114</Volume>
<Issue>5</Issue>
<PubDate><Year>2017</Year>
<Month>01</Month>
<Day>31</Day>
</PubDate>
</JournalIssue>
<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation>
</Journal>
<ArticleTitle>TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity.</ArticleTitle>
<Pagination><MedlinePgn>1039-1044</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1615093114</ELocationID>
<Abstract><AbstractText>Maintaining cellular homeostasis under changing nutrient conditions is essential for the growth and development of all organisms. The mechanisms that maintain homeostasis upon loss of nutrient supply are not well understood. By mapping the SUMO proteome in Saccharomyces cerevisiae, we discovered a specific set of differentially sumoylated proteins mainly involved in transcription. RNA polymerase III (RNAPIII) components, including Rpc53, Rpc82, and Ret1, are particularly prominent nutrient-dependent SUMO targets. Nitrogen starvation, as well as direct inhibition of the master nutrient response regulator target of rapamycin complex 1 (TORC1), results in rapid desumoylation of these proteins, which is reflected by loss of SUMO at tRNA genes. TORC1-dependent sumoylation of Rpc82 in particular is required for robust tRNA transcription. Mechanistically, sumoylation of Rpc82 is important for assembly of the RNAPIII holoenzyme and recruitment of Rpc82 to tRNA genes. In conclusion, our data show that TORC1-dependent sumoylation of Rpc82 bolsters the transcriptional capacity of RNAPIII under optimal growth conditions.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chymkowitch</LastName>
<ForeName>Pierre</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway; jorrit.enserink@rr-research.no pierre.chymkowitch@rr-research.no.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Section for Biochemistry and Molecular Biology, The Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, NO-0371 Oslo, Norway.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Microbiology, Oslo University Hospital, NO-0027 Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Nguéa P</LastName>
<ForeName>Aurélie</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Section for Biochemistry and Molecular Biology, The Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, NO-0371 Oslo, Norway.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Microbiology, Oslo University Hospital, NO-0027 Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Aanes</LastName>
<ForeName>Håvard</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, Oslo University Hospital, NO-0027 Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Robertson</LastName>
<ForeName>Joseph</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Section for Biochemistry and Molecular Biology, The Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, NO-0371 Oslo, Norway.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Microbiology, Oslo University Hospital, NO-0027 Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Klungland</LastName>
<ForeName>Arne</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Microbiology, Oslo University Hospital, NO-0027 Oslo, Norway.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, NO-0317 Oslo, Norway.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Enserink</LastName>
<ForeName>Jorrit M</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Cell Biology, Institute for Cancer Research, Oslo University Hospital, NO-0379 Oslo, Norway; jorrit.enserink@rr-research.no pierre.chymkowitch@rr-research.no.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Section for Biochemistry and Molecular Biology, The Department of Biosciences, Faculty of Mathematics and Natural Sciences, University of Oslo, NO-0371 Oslo, Norway.</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>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>01</Month>
<Day>17</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Proc Natl Acad Sci U S A</MedlineTA>
<NlmUniqueID>7505876</NlmUniqueID>
<ISSNLinking>0027-8424</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012331">RNA, Fungal</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C561842">TORC1 protein complex, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>9014-25-9</RegistryNumber>
<NameOfSubstance UI="D012343">RNA, Transfer</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.3.2.23</RegistryNumber>
<NameOfSubstance UI="D044763">Ubiquitin-Conjugating Enzymes</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.7.6</RegistryNumber>
<NameOfSubstance UI="D012320">RNA Polymerase III</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.7.6</RegistryNumber>
<NameOfSubstance UI="C000626844">RPC82 protein, S cerevisiae</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 6.3.2.-</RegistryNumber>
<NameOfSubstance UI="C091170">ubiquitin-conjugating enzyme UBC9</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>N762921K75</RegistryNumber>
<NameOfSubstance UI="D009584">Nitrogen</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber>
<NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D063990" MajorTopicYN="N">Gene Ontology</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012320" MajorTopicYN="N">RNA Polymerase III</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012331" MajorTopicYN="N">RNA, Fungal</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012343" MajorTopicYN="N">RNA, Transfer</DescriptorName>
<QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020123" MajorTopicYN="N">Sirolimus</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D058207" MajorTopicYN="N">Sumoylation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014158" MajorTopicYN="Y">Transcription, Genetic</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D044763" MajorTopicYN="N">Ubiquitin-Conjugating Enzymes</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">RNA polymerase III</Keyword>
<Keyword MajorTopicYN="Y">Sumo</Keyword>
<Keyword MajorTopicYN="Y">TORC1</Keyword>
<Keyword MajorTopicYN="Y">tRNA</Keyword>
<Keyword MajorTopicYN="Y">transcription</Keyword>
</KeywordList>
<CoiStatement>The authors declare no conflict of interest.</CoiStatement>
</MedlineCitation>
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TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity.

TORC1-dependent sumoylation of Rpc82 promotes RNA polymerase III assembly and activity.

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