Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae.
Identifieur interne : 001747 ( Main/Exploration ); précédent : 001746; suivant : 001748Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae.
Auteurs : André Feller [Belgique] ; Mélanie Boeckstaens ; Anna Maria Marini ; Evelyne DuboisSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2006.
Descripteurs français
- KwdFr :
- Azote (composition chimique), Azote (métabolisme), Complexes de tri endosomique requis pour le transport (MeSH), Cytosol (métabolisme), Facteurs de transcription (métabolisme), Facteurs de transcription (physiologie), Protein kinases (métabolisme), Protéines adaptatrices de la transduction du signal (métabolisme), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de Saccharomyces cerevisiae (physiologie), Protéines de répression (métabolisme), Protéines de répression (physiologie), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (métabolisme), Transcription génétique (MeSH), Transport biologique (MeSH), Transport nucléaire actif (MeSH), Ubiquitin-protein ligase complexes (métabolisme), Ubiquitin-protein ligases (MeSH).
- MESH :
- composition chimique : Azote.
- métabolisme : Azote, Cytosol, Facteurs de transcription, Protein kinases, Protéines adaptatrices de la transduction du signal, Protéines de Saccharomyces cerevisiae, Protéines de répression, Saccharomyces cerevisiae, Ubiquitin-protein ligase complexes.
- physiologie : Facteurs de transcription, Protéines de Saccharomyces cerevisiae, Protéines de répression.
- Complexes de tri endosomique requis pour le transport, Régulation de l'expression des gènes fongiques, Transcription génétique, Transport biologique, Transport nucléaire actif, Ubiquitin-protein ligases.
English descriptors
- KwdEn :
- Active Transport, Cell Nucleus (MeSH), Adaptor Proteins, Signal Transducing (metabolism), Biological Transport (MeSH), Cytosol (metabolism), Endosomal Sorting Complexes Required for Transport (MeSH), Gene Expression Regulation, Fungal (MeSH), Nitrogen (chemistry), Nitrogen (metabolism), Protein Kinases (metabolism), Repressor Proteins (metabolism), Repressor Proteins (physiology), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Saccharomyces cerevisiae Proteins (physiology), Transcription Factors (metabolism), Transcription Factors (physiology), Transcription, Genetic (MeSH), Ubiquitin-Protein Ligase Complexes (metabolism), Ubiquitin-Protein Ligases (MeSH).
- MESH :
- chemical , chemistry : Nitrogen.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Nitrogen, Protein Kinases, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Ubiquitin-Protein Ligase Complexes.
- metabolism : Cytosol, Saccharomyces cerevisiae.
- chemical , physiology : Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- Active Transport, Cell Nucleus, Biological Transport, Endosomal Sorting Complexes Required for Transport, Gene Expression Regulation, Fungal, Transcription, Genetic, Ubiquitin-Protein Ligases.
Abstract
Nitrogen Catabolite Repression (NCR) allows the adaptation of yeast cells to the quality of nitrogen supply by inhibiting the transcription of genes encoding proteins involved in transport and degradation of nonpreferred nitrogen sources. In cells using ammonium or glutamine, the GATA transcription factor Gln3 is sequestered in the cytoplasm by Ure2 whereas it enters the nucleus after a shift to a nonpreferred nitrogen source like proline or upon addition of rapamycin, the TOR complex inhibitor. Recently, the Npr1 kinase and the Rsp5, Bul1/2 ubiquitin ligase complex were reported to have antagonistic roles in the nuclear import and Gln3-mediated activation. The Npr1 kinase controls the activity of various permeases including transporters for nitrogen sources that stimulate NCR such as the Mep ammonium transport systems. Combining data from growth tests, Northern blot analysis and Gln3 immunolocalization, we show that the Npr1 kinase is not a direct negative regulator of Gln3-dependent transcription. The derepression of Gln3-activated genes in ammonium-grown npr1 cells results from the reduced uptake of the nitrogen-repressing compound because NCR could be restored in npr1 cells by repairing ammonium-uptake defects through different means. Finally, we show that the impairment of the ubiquitin ligase complex does not prevent induction of NCR genes under nonpreferred nitrogen conditions. The apparent Rsp5-, Bul1/2-dependent Gln3 activation keeps to the cellular status, as it is only observed in cells having left the balanced phase of exponential growth.
DOI: 10.1074/jbc.M605551200
PubMed: 16864574
Affiliations:
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(metabolism)</term><term>Ubiquitin-Protein Ligases (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Azote (composition chimique)</term><term>Azote (métabolisme)</term><term>Complexes de tri endosomique requis pour le transport (MeSH)</term><term>Cytosol (métabolisme)</term><term>Facteurs de transcription (métabolisme)</term><term>Facteurs de transcription (physiologie)</term><term>Protein kinases (métabolisme)</term><term>Protéines adaptatrices de la transduction du signal (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (physiologie)</term><term>Protéines de répression (métabolisme)</term><term>Protéines de répression (physiologie)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Transcription génétique (MeSH)</term><term>Transport biologique (MeSH)</term><term>Transport nucléaire actif (MeSH)</term><term>Ubiquitin-protein ligase complexes (métabolisme)</term><term>Ubiquitin-protein ligases (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Nitrogen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Nitrogen</term><term>Protein Kinases</term><term>Repressor Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term><term>Ubiquitin-Protein Ligase Complexes</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Azote</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Azote</term><term>Cytosol</term><term>Facteurs de transcription</term><term>Protein kinases</term><term>Protéines adaptatrices de la transduction du signal</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de répression</term><term>Saccharomyces cerevisiae</term><term>Ubiquitin-protein ligase complexes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Facteurs de transcription</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de répression</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Repressor Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term><term>Biological Transport</term><term>Endosomal Sorting Complexes Required for Transport</term><term>Gene Expression Regulation, Fungal</term><term>Transcription, Genetic</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Complexes de tri endosomique requis pour le transport</term><term>Régulation de l'expression des gènes fongiques</term><term>Transcription génétique</term><term>Transport biologique</term><term>Transport nucléaire actif</term><term>Ubiquitin-protein ligases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nitrogen Catabolite Repression (NCR) allows the adaptation of yeast cells to the quality of nitrogen supply by inhibiting the transcription of genes encoding proteins involved in transport and degradation of nonpreferred nitrogen sources. In cells using ammonium or glutamine, the GATA transcription factor Gln3 is sequestered in the cytoplasm by Ure2 whereas it enters the nucleus after a shift to a nonpreferred nitrogen source like proline or upon addition of rapamycin, the TOR complex inhibitor. Recently, the Npr1 kinase and the Rsp5, Bul1/2 ubiquitin ligase complex were reported to have antagonistic roles in the nuclear import and Gln3-mediated activation. The Npr1 kinase controls the activity of various permeases including transporters for nitrogen sources that stimulate NCR such as the Mep ammonium transport systems. Combining data from growth tests, Northern blot analysis and Gln3 immunolocalization, we show that the Npr1 kinase is not a direct negative regulator of Gln3-dependent transcription. The derepression of Gln3-activated genes in ammonium-grown npr1 cells results from the reduced uptake of the nitrogen-repressing compound because NCR could be restored in npr1 cells by repairing ammonium-uptake defects through different means. Finally, we show that the impairment of the ubiquitin ligase complex does not prevent induction of NCR genes under nonpreferred nitrogen conditions. The apparent Rsp5-, Bul1/2-dependent Gln3 activation keeps to the cellular status, as it is only observed in cells having left the balanced phase of exponential growth.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16864574</PMID><DateCompleted><Year>2006</Year><Month>11</Month><Day>27</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>281</Volume><Issue>39</Issue><PubDate><Year>2006</Year><Month>Sep</Month><Day>29</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>28546-54</MedlinePgn></Pagination><Abstract><AbstractText>Nitrogen Catabolite Repression (NCR) allows the adaptation of yeast cells to the quality of nitrogen supply by inhibiting the transcription of genes encoding proteins involved in transport and degradation of nonpreferred nitrogen sources. In cells using ammonium or glutamine, the GATA transcription factor Gln3 is sequestered in the cytoplasm by Ure2 whereas it enters the nucleus after a shift to a nonpreferred nitrogen source like proline or upon addition of rapamycin, the TOR complex inhibitor. Recently, the Npr1 kinase and the Rsp5, Bul1/2 ubiquitin ligase complex were reported to have antagonistic roles in the nuclear import and Gln3-mediated activation. The Npr1 kinase controls the activity of various permeases including transporters for nitrogen sources that stimulate NCR such as the Mep ammonium transport systems. Combining data from growth tests, Northern blot analysis and Gln3 immunolocalization, we show that the Npr1 kinase is not a direct negative regulator of Gln3-dependent transcription. The derepression of Gln3-activated genes in ammonium-grown npr1 cells results from the reduced uptake of the nitrogen-repressing compound because NCR could be restored in npr1 cells by repairing ammonium-uptake defects through different means. Finally, we show that the impairment of the ubiquitin ligase complex does not prevent induction of NCR genes under nonpreferred nitrogen conditions. The apparent Rsp5-, Bul1/2-dependent Gln3 activation keeps to the cellular status, as it is only observed in cells having left the balanced phase of exponential growth.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Feller</LastName><ForeName>André</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institut de Recherches Microbiologiques J-M Wiame, Laboratoire de Microbiologie, Université Libre de Bruxelles, 1070 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boeckstaens</LastName><ForeName>Mélanie</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Marini</LastName><ForeName>Anna Maria</ForeName><Initials>AM</Initials></Author><Author ValidYN="Y"><LastName>Dubois</LastName><ForeName>Evelyne</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType 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UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012097">Repressor Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>147682-31-3</RegistryNumber><NameOfSubstance UI="C066958">NPR1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.23</RegistryNumber><NameOfSubstance UI="D043743">Ubiquitin-Protein Ligase Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance UI="D044767">Ubiquitin-Protein Ligases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 6.3.2.-</RegistryNumber><NameOfSubstance UI="C469287">RSP5 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>N762921K75</RegistryNumber><NameOfSubstance UI="D009584">Nitrogen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D021581" MajorTopicYN="N">Active Transport, Cell Nucleus</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D056827" MajorTopicYN="N">Endosomal Sorting Complexes Required for Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="Y">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009584" MajorTopicYN="N">Nitrogen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012097" MajorTopicYN="N">Repressor Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="Y">Transcription, Genetic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D043743" MajorTopicYN="N">Ubiquitin-Protein Ligase Complexes</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>7</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2006</Year><Month>12</Month><Day>9</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>7</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16864574</ArticleId><ArticleId IdType="pii">M605551200</ArticleId><ArticleId IdType="doi">10.1074/jbc.M605551200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Belgique</li></country><region><li>Région de Bruxelles-Capitale</li></region><settlement><li>Bruxelles</li></settlement><orgName><li>Université libre de Bruxelles</li></orgName></list><tree><noCountry><name sortKey="Boeckstaens, Melanie" sort="Boeckstaens, Melanie" uniqKey="Boeckstaens M" first="Mélanie" last="Boeckstaens">Mélanie Boeckstaens</name><name sortKey="Dubois, Evelyne" sort="Dubois, Evelyne" uniqKey="Dubois E" first="Evelyne" last="Dubois">Evelyne Dubois</name><name sortKey="Marini, Anna Maria" sort="Marini, Anna Maria" uniqKey="Marini A" first="Anna Maria" last="Marini">Anna Maria Marini</name></noCountry><country name="Belgique"><region name="Région de Bruxelles-Capitale"><name sortKey="Feller, Andre" sort="Feller, Andre" uniqKey="Feller A" first="André" last="Feller">André Feller</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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