The tor pathway regulates gene expression by linking nutrient sensing to histone acetylation.
Identifieur interne : 001915 ( Main/Exploration ); précédent : 001914; suivant : 001916The tor pathway regulates gene expression by linking nutrient sensing to histone acetylation.
Auteurs : John R. Rohde [États-Unis] ; Maria E. CardenasSource :
- Molecular and cellular biology [ 0270-7306 ] ; 2003.
Descripteurs français
- KwdFr :
- Acétylation (MeSH), Antifongiques (pharmacologie), Chromatine (métabolisme), Facteurs de transcription (métabolisme), Facteurs temps (MeSH), Histone (métabolisme), Histone deacetylases (MeSH), Liaison aux protéines (MeSH), Modèles génétiques (MeSH), Phosphatidylinositol 3-kinases (métabolisme), Phosphatidylinositol 3-kinases (physiologie), Phosphotransferases (Alcohol Group Acceptor) (métabolisme), Phosphotransferases (Alcohol Group Acceptor) (physiologie), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de Saccharomyces cerevisiae (physiologie), Protéines de liaison à l'ADN (métabolisme), Protéines télomériques (métabolisme), Réactifs réticulants (pharmacologie), Régions promotrices (génétique) (MeSH), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Technique de Northern (MeSH), Technique de Western (MeSH), Tests aux précipitines (MeSH), Transduction du signal (MeSH).
- MESH :
- métabolisme : Chromatine, Facteurs de transcription, Histone, Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae, Protéines de liaison à l'ADN, Protéines télomériques, Saccharomyces cerevisiae.
- pharmacologie : Antifongiques, Réactifs réticulants, Sirolimus.
- physiologie : Phosphatidylinositol 3-kinases, Phosphotransferases (Alcohol Group Acceptor), Protéines de Saccharomyces cerevisiae.
- Acétylation, Facteurs temps, Histone deacetylases, Liaison aux protéines, Modèles génétiques, Régions promotrices (génétique), Régulation de l'expression des gènes fongiques, Technique de Northern, Technique de Western, Tests aux précipitines, Transduction du signal.
English descriptors
- KwdEn :
- Acetylation (MeSH), Antifungal Agents (pharmacology), Blotting, Northern (MeSH), Blotting, Western (MeSH), Chromatin (metabolism), Cross-Linking Reagents (pharmacology), DNA-Binding Proteins (metabolism), Gene Expression Regulation, Fungal (MeSH), Histone Deacetylases (MeSH), Histones (metabolism), Models, Genetic (MeSH), Phosphatidylinositol 3-Kinases (metabolism), Phosphatidylinositol 3-Kinases (physiology), Phosphotransferases (Alcohol Group Acceptor) (metabolism), Phosphotransferases (Alcohol Group Acceptor) (physiology), Precipitin Tests (MeSH), Promoter Regions, Genetic (MeSH), Protein Binding (MeSH), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (physiology), Signal Transduction (MeSH), Sirolimus (pharmacology), Telomere-Binding Proteins (metabolism), Time Factors (MeSH), Transcription Factors (metabolism).
- MESH :
- chemical , metabolism : Chromatin, DNA-Binding Proteins, Histones, Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins, Telomere-Binding Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents, Cross-Linking Reagents, Sirolimus.
- chemical , physiology : Phosphatidylinositol 3-Kinases, Phosphotransferases (Alcohol Group Acceptor), Saccharomyces cerevisiae Proteins.
- metabolism : Saccharomyces cerevisiae.
- Acetylation, Blotting, Northern, Blotting, Western, Gene Expression Regulation, Fungal, Histone Deacetylases, Models, Genetic, Precipitin Tests, Promoter Regions, Genetic, Protein Binding, Signal Transduction, Time Factors.
Abstract
The Tor pathway mediates cell growth in response to nutrient availability, in part by inducing ribosomal protein (RP) gene expression via an unknown mechanism. Expression of RP genes coincides with recruitment of the Esa1 histone acetylase to RP gene promoters. We show that inhibition of Tor with rapamycin releases Esa1 from RP gene promoters and leads to histone H4 deacetylation without affecting promoter occupancy by Rap1 and Abf1. Genetic and biochemical evidence identifies Rpd3 as the major histone deacetylase responsible for reversing histone H4 acetylation at RP gene promoters in response to Tor inhibition by rapamycin or nutrient limitation. Our results illustrate that the Tor pathway links nutrient sensing with histone acetylation to control RP gene expression and cell growth.
DOI: 10.1128/mcb.23.2.629-635.2003
PubMed: 12509460
PubMed Central: PMC151550
Affiliations:
Links toward previous steps (curation, corpus...)
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scheme="MESH" xml:lang="fr"><term>Acétylation</term><term>Facteurs temps</term><term>Histone deacetylases</term><term>Liaison aux protéines</term><term>Modèles génétiques</term><term>Régions promotrices (génétique)</term><term>Régulation de l'expression des gènes fongiques</term><term>Technique de Northern</term><term>Technique de Western</term><term>Tests aux précipitines</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The Tor pathway mediates cell growth in response to nutrient availability, in part by inducing ribosomal protein (RP) gene expression via an unknown mechanism. Expression of RP genes coincides with recruitment of the Esa1 histone acetylase to RP gene promoters. We show that inhibition of Tor with rapamycin releases Esa1 from RP gene promoters and leads to histone H4 deacetylation without affecting promoter occupancy by Rap1 and Abf1. Genetic and biochemical evidence identifies Rpd3 as the major histone deacetylase responsible for reversing histone H4 acetylation at RP gene promoters in response to Tor inhibition by rapamycin or nutrient limitation. Our results illustrate that the Tor pathway links nutrient sensing with histone acetylation to control RP gene expression and cell growth.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12509460</PMID><DateCompleted><Year>2003</Year><Month>02</Month><Day>24</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>23</Volume><Issue>2</Issue><PubDate><Year>2003</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>The tor pathway regulates gene expression by linking nutrient sensing to histone acetylation.</ArticleTitle><Pagination><MedlinePgn>629-35</MedlinePgn></Pagination><Abstract><AbstractText>The Tor pathway mediates cell growth in response to nutrient availability, in part by inducing ribosomal protein (RP) gene expression via an unknown mechanism. Expression of RP genes coincides with recruitment of the Esa1 histone acetylase to RP gene promoters. We show that inhibition of Tor with rapamycin releases Esa1 from RP gene promoters and leads to histone H4 deacetylation without affecting promoter occupancy by Rap1 and Abf1. Genetic and biochemical evidence identifies Rpd3 as the major histone deacetylase responsible for reversing histone H4 acetylation at RP gene promoters in response to Tor inhibition by rapamycin or nutrient limitation. Our results illustrate that the Tor pathway links nutrient sensing with histone acetylation to control RP gene expression and cell growth.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rohde</LastName><ForeName>John R</ForeName><Initials>JR</Initials><AffiliationInfo><Affiliation>Department of Molecular Genetics and Microbiology, Duke University Medical Center, Durham, North Carolina 27710, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cardenas</LastName><ForeName>Maria E</ForeName><Initials>ME</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>K22 CA094925</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>K22 CA94925-01</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal 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