Repression of yeast RNA polymerase III by stress leads to ubiquitylation and proteasomal degradation of its largest subunit, C160.
Identifieur interne : 000247 ( Main/Exploration ); précédent : 000246; suivant : 000248Repression of yeast RNA polymerase III by stress leads to ubiquitylation and proteasomal degradation of its largest subunit, C160.
Auteurs : Ewa Le Niewska [Pologne] ; Małgorzata Cie La [Pologne] ; Magdalena Boguta [Pologne]Source :
- Biochimica et biophysica acta. Gene regulatory mechanisms [ 1876-4320 ] ; 2019.
Descripteurs français
- KwdFr :
- Proteasome endopeptidase complex (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), RNA polymerase III (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (physiologie), Sous-unités de protéines (métabolisme), Stress physiologique (physiologie), Transcription génétique (MeSH), Ubiquitination (MeSH).
- MESH :
- génétique : Saccharomyces cerevisiae.
- métabolisme : Proteasome endopeptidase complex, Protéines de Saccharomyces cerevisiae, RNA polymerase III, Sous-unités de protéines.
- physiologie : Saccharomyces cerevisiae, Stress physiologique.
- Transcription génétique, Ubiquitination.
English descriptors
- KwdEn :
- Proteasome Endopeptidase Complex (metabolism), Protein Subunits (metabolism), RNA Polymerase III (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (physiology), Saccharomyces cerevisiae Proteins (metabolism), Stress, Physiological (physiology), Transcription, Genetic (MeSH), Ubiquitination (MeSH).
- MESH :
- chemical , metabolism : Proteasome Endopeptidase Complex, Protein Subunits, RNA Polymerase III, Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae.
- physiology : Saccharomyces cerevisiae, Stress, Physiological.
- Transcription, Genetic, Ubiquitination.
Abstract
Respiratory growth and various stress conditions repress RNA polymerase III (Pol III) transcription in Saccharomyces cerevisiae. Here we report a degradation of the largest Pol III catalytic subunit, C160 as a consequence of Pol III transcription repression. We observed C160 degradation in response to transfer of yeast from fermentation to respiration conditions, as well as treatment with rapamycin or inhibition of nucleotide biosynthesis. We also detected ubiquitylated forms of C160 and demonstrated that C160 protein degradation is dependent on proteasome activity. A comparable time-course study of Pol III repression upon metabolic shift from fermentation to respiration shows that the transcription inhibition is correlated with Pol III dissociation from chromatin but that the degradation of C160 subunit is a downstream event. Despite blocking degradation of C160 by proteasome, Pol III-transcribed genes are under proper regulation. We postulate that the degradation of C160 is activated under stress conditions to reduce the amount of existing Pol III complex and prevent its de novo assembly.
DOI: 10.1016/j.bbagrm.2018.10.007
PubMed: 30342998
Affiliations:
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Here we report a degradation of the largest Pol III catalytic subunit, C160 as a consequence of Pol III transcription repression. We observed C160 degradation in response to transfer of yeast from fermentation to respiration conditions, as well as treatment with rapamycin or inhibition of nucleotide biosynthesis. We also detected ubiquitylated forms of C160 and demonstrated that C160 protein degradation is dependent on proteasome activity. A comparable time-course study of Pol III repression upon metabolic shift from fermentation to respiration shows that the transcription inhibition is correlated with Pol III dissociation from chromatin but that the degradation of C160 subunit is a downstream event. Despite blocking degradation of C160 by proteasome, Pol III-transcribed genes are under proper regulation. We postulate that the degradation of C160 is activated under stress conditions to reduce the amount of existing Pol III complex and prevent its de novo assembly.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30342998</PMID><DateCompleted><Year>2019</Year><Month>08</Month><Day>12</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1876-4320</ISSN><JournalIssue CitedMedium="Internet"><Volume>1862</Volume><Issue>1</Issue><PubDate><Year>2019</Year><Month>01</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Gene regulatory mechanisms</Title><ISOAbbreviation>Biochim Biophys Acta Gene Regul Mech</ISOAbbreviation></Journal><ArticleTitle>Repression of yeast RNA polymerase III by stress leads to ubiquitylation and proteasomal degradation of its largest subunit, C160.</ArticleTitle><Pagination><MedlinePgn>25-34</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1874-9399(18)30236-0</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagrm.2018.10.007</ELocationID><Abstract><AbstractText>Respiratory growth and various stress conditions repress RNA polymerase III (Pol III) transcription in Saccharomyces cerevisiae. Here we report a degradation of the largest Pol III catalytic subunit, C160 as a consequence of Pol III transcription repression. We observed C160 degradation in response to transfer of yeast from fermentation to respiration conditions, as well as treatment with rapamycin or inhibition of nucleotide biosynthesis. We also detected ubiquitylated forms of C160 and demonstrated that C160 protein degradation is dependent on proteasome activity. A comparable time-course study of Pol III repression upon metabolic shift from fermentation to respiration shows that the transcription inhibition is correlated with Pol III dissociation from chromatin but that the degradation of C160 subunit is a downstream event. Despite blocking degradation of C160 by proteasome, Pol III-transcribed genes are under proper regulation. We postulate that the degradation of C160 is activated under stress conditions to reduce the amount of existing Pol III complex and prevent its de novo assembly.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Leśniewska</LastName><ForeName>Ewa</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cieśla</LastName><ForeName>Małgorzata</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boguta</LastName><ForeName>Magdalena</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5A, 02-106 Warsaw, Poland. Electronic address: magda@ibb.waw.pl.</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>2018</Year><Month>10</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Gene Regul Mech</MedlineTA><NlmUniqueID>101731723</NlmUniqueID><ISSNLinking>1874-9399</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.7.6</RegistryNumber><NameOfSubstance UI="D012320">RNA Polymerase III</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance></Chemical></ChemicalList><MeshHeadingList><MeshHeading><DescriptorName UI="D046988" MajorTopicYN="N">Proteasome Endopeptidase Complex</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021122" MajorTopicYN="N">Protein Subunits</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012320" MajorTopicYN="N">RNA Polymerase III</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013312" MajorTopicYN="N">Stress, Physiological</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054875" MajorTopicYN="N">Ubiquitination</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>05</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>10</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>10</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>10</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>8</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>10</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">30342998</ArticleId><ArticleId IdType="pii">S1874-9399(18)30236-0</ArticleId><ArticleId IdType="doi">10.1016/j.bbagrm.2018.10.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Pologne</li></country></list><tree><country name="Pologne"><noRegion><name sortKey="Le Niewska, Ewa" sort="Le Niewska, Ewa" uniqKey="Le Niewska E" first="Ewa" last="Le Niewska">Ewa Le Niewska</name></noRegion><name sortKey="Boguta, Magdalena" sort="Boguta, Magdalena" uniqKey="Boguta M" first="Magdalena" last="Boguta">Magdalena Boguta</name><name sortKey="Cie La, Malgorzata" sort="Cie La, Malgorzata" uniqKey="Cie La M" first="Małgorzata" last="Cie La">Małgorzata Cie La</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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