Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway.
Identifieur interne : 001A72 ( Main/Exploration ); précédent : 001A71; suivant : 001A73Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway.
Auteurs : D. Zaragoza [Canada] ; A. Ghavidel ; J. Heitman ; M C SchultzSource :
- Molecular and cellular biology [ 0270-7306 ] ; 1998.
Descripteurs français
- KwdFr :
- Antifongiques (pharmacologie), Biosynthèse des protéines (MeSH), Phase G0 (MeSH), Phase G1 (MeSH), Phosphatidylinositol 3-kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (antagonistes et inhibiteurs), Phosphotransferases (Alcohol Group Acceptor) (génétique), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Polyènes (pharmacologie), Protéines de Saccharomyces cerevisiae (MeSH), Protéines du cycle cellulaire (MeSH), RNA polymerase III (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Sirolimus (MeSH), Température (MeSH), Transcription génétique (effets des médicaments et des substances chimiques), Transduction du signal (effets des médicaments et des substances chimiques).
- MESH :
- antagonistes et inhibiteurs : Phosphotransferases (Alcohol Group Acceptor).
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques, Saccharomyces cerevisiae, Transcription génétique, Transduction du signal.
- génétique : Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae.
- métabolisme : Phosphotransferases (Alcohol Group Acceptor), RNA polymerase III.
- pharmacologie : Antifongiques, Polyènes.
- Biosynthèse des protéines, Phase G0, Phase G1, Phosphatidylinositol 3-kinases, Protéines de Saccharomyces cerevisiae, Protéines du cycle cellulaire, Sirolimus, Température.
English descriptors
- KwdEn :
- Antifungal Agents (pharmacology), Cell Cycle Proteins (MeSH), G1 Phase (MeSH), Gene Expression Regulation, Fungal (drug effects), Phosphatidylinositol 3-Kinases (MeSH), Phosphotransferases (Alcohol Group Acceptor) (antagonists & inhibitors), Phosphotransferases (Alcohol Group Acceptor) (genetics), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Polyenes (pharmacology), Protein Biosynthesis (MeSH), RNA Polymerase III (metabolism), Resting Phase, Cell Cycle (MeSH), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (MeSH), Signal Transduction (drug effects), Sirolimus (MeSH), Temperature (MeSH), Transcription, Genetic (drug effects).
- MESH :
- chemical , antagonists & inhibitors : Phosphotransferases (Alcohol Group Acceptor).
- chemical , genetics : Phosphotransferases (Alcohol Group Acceptor).
- chemical , metabolism : Phosphotransferases (Alcohol Group Acceptor), RNA Polymerase III.
- chemical , pharmacology : Antifungal Agents, Polyenes.
- chemical : Cell Cycle Proteins, Phosphatidylinositol 3-Kinases, Saccharomyces cerevisiae Proteins, Sirolimus.
- drug effects : Gene Expression Regulation, Fungal, Saccharomyces cerevisiae, Signal Transduction, Transcription, Genetic.
- genetics : Saccharomyces cerevisiae.
- G1 Phase, Protein Biosynthesis, Resting Phase, Cell Cycle, Temperature.
Abstract
The macrolide antibiotic rapamycin inhibits cellular proliferation by interfering with the highly conserved TOR (for target of rapamycin) signaling pathway. Growth arrest of budding yeast cells treated with rapamycin is followed by the program of molecular events that characterizes entry into G0 (stationary phase), including the induction of polymerase (Pol) II genes typically expressed only in G0. Normally, progression into G0 is characterized by transcriptional repression of the Pol I and III genes. Here, we show that rapamycin treatment also causes the transcriptional repression of Pol I and III genes. The down-regulation of Pol III transcription is TOR dependent. While it coincides with translational repression by rapamycin, transcriptional repression is due in part to a translation-independent effect that is evident in extracts from a conditional tor2 mutant. Biochemical experiments reveal that RNA Pol III and probably transcription initiation factor TFIIIB are targets of repression by rapamycin. In view of previous evidence that TFIIIB and Pol III are inhibited when protein phosphatase 2A (PP2A) function is impaired, and that PP2A is a component of the TOR pathway, our results suggest that TOR signaling regulates Pol I and Pol III transcription in response to nutrient growth signals.
DOI: 10.1128/mcb.18.8.4463
PubMed: 9671456
PubMed Central: PMC109032
Affiliations:
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cellulaire</term><term>Sirolimus</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The macrolide antibiotic rapamycin inhibits cellular proliferation by interfering with the highly conserved TOR (for target of rapamycin) signaling pathway. Growth arrest of budding yeast cells treated with rapamycin is followed by the program of molecular events that characterizes entry into G0 (stationary phase), including the induction of polymerase (Pol) II genes typically expressed only in G0. Normally, progression into G0 is characterized by transcriptional repression of the Pol I and III genes. Here, we show that rapamycin treatment also causes the transcriptional repression of Pol I and III genes. The down-regulation of Pol III transcription is TOR dependent. While it coincides with translational repression by rapamycin, transcriptional repression is due in part to a translation-independent effect that is evident in extracts from a conditional tor2 mutant. Biochemical experiments reveal that RNA Pol III and probably transcription initiation factor TFIIIB are targets of repression by rapamycin. In view of previous evidence that TFIIIB and Pol III are inhibited when protein phosphatase 2A (PP2A) function is impaired, and that PP2A is a component of the TOR pathway, our results suggest that TOR signaling regulates Pol I and Pol III transcription in response to nutrient growth signals.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9671456</PMID><DateCompleted><Year>1998</Year><Month>08</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0270-7306</ISSN><JournalIssue CitedMedium="Print"><Volume>18</Volume><Issue>8</Issue><PubDate><Year>1998</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Rapamycin induces the G0 program of transcriptional repression in yeast by interfering with the TOR signaling pathway.</ArticleTitle><Pagination><MedlinePgn>4463-70</MedlinePgn></Pagination><Abstract><AbstractText>The macrolide antibiotic rapamycin inhibits cellular proliferation by interfering with the highly conserved TOR (for target of rapamycin) signaling pathway. Growth arrest of budding yeast cells treated with rapamycin is followed by the program of molecular events that characterizes entry into G0 (stationary phase), including the induction of polymerase (Pol) II genes typically expressed only in G0. Normally, progression into G0 is characterized by transcriptional repression of the Pol I and III genes. Here, we show that rapamycin treatment also causes the transcriptional repression of Pol I and III genes. The down-regulation of Pol III transcription is TOR dependent. While it coincides with translational repression by rapamycin, transcriptional repression is due in part to a translation-independent effect that is evident in extracts from a conditional tor2 mutant. Biochemical experiments reveal that RNA Pol III and probably transcription initiation factor TFIIIB are targets of repression by rapamycin. In view of previous evidence that TFIIIB and Pol III are inhibited when protein phosphatase 2A (PP2A) function is impaired, and that PP2A is a component of the TOR pathway, our results suggest that TOR signaling regulates Pol I and Pol III transcription in response to nutrient growth signals.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zaragoza</LastName><ForeName>D</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada T6G 2H7.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ghavidel</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Heitman</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Schultz</LastName><ForeName>M C</ForeName><Initials>MC</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal 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Ghavidel</name><name sortKey="Heitman, J" sort="Heitman, J" uniqKey="Heitman J" first="J" last="Heitman">J. Heitman</name><name sortKey="Schultz, M C" sort="Schultz, M C" uniqKey="Schultz M" first="M C" last="Schultz">M C Schultz</name></noCountry><country name="Canada"><noRegion><name sortKey="Zaragoza, D" sort="Zaragoza, D" uniqKey="Zaragoza D" first="D" last="Zaragoza">D. Zaragoza</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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