Nitrogen-responsive regulation of GATA protein family activators Gln3 and Gat1 occurs by two distinct pathways, one inhibited by rapamycin and the other by methionine sulfoximine.
Identifieur interne : 001283 ( Main/Exploration ); précédent : 001282; suivant : 001284Nitrogen-responsive regulation of GATA protein family activators Gln3 and Gat1 occurs by two distinct pathways, one inhibited by rapamycin and the other by methionine sulfoximine.
Auteurs : Isabelle Georis [Belgique] ; Jennifer J. Tate ; Terrance G. Cooper ; Evelyne DuboisSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2011.
Descripteurs français
- KwdFr :
- Antifongiques (pharmacologie), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Facteurs de transcription GATA (génétique), Facteurs de transcription GATA (métabolisme), Glutamine (génétique), Glutamine (métabolisme), Méthionine sulfoximine (pharmacologie), Noyau de la cellule (génétique), Noyau de la cellule (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Régulation de l'expression des gènes fongiques (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Éléments de réponse (physiologie).
- MESH :
- effets des médicaments et des substances chimiques : Régulation de l'expression des gènes fongiques.
- génétique : Facteurs de transcription, Facteurs de transcription GATA, Glutamine, Noyau de la cellule, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Facteurs de transcription, Facteurs de transcription GATA, Glutamine, Noyau de la cellule, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Antifongiques, Méthionine sulfoximine, Sirolimus.
- physiologie : Éléments de réponse.
English descriptors
- KwdEn :
- Antifungal Agents (pharmacology), Cell Nucleus (genetics), Cell Nucleus (metabolism), GATA Transcription Factors (genetics), GATA Transcription Factors (metabolism), Gene Expression Regulation, Fungal (drug effects), Glutamine (genetics), Glutamine (metabolism), Methionine Sulfoximine (pharmacology), Response Elements (physiology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : GATA Transcription Factors, Glutamine, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : GATA Transcription Factors, Glutamine, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Antifungal Agents, Methionine Sulfoximine, Sirolimus.
- drug effects : Gene Expression Regulation, Fungal.
- genetics : Cell Nucleus, Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, Saccharomyces cerevisiae.
- physiology : Response Elements.
Abstract
Nitrogen availability regulates the transcription of genes required to degrade non-preferentially utilized nitrogen sources by governing the localization and function of transcription activators, Gln3 and Gat1. TorC1 inhibitor, rapamycin (Rap), and glutamine synthetase inhibitor, methionine sulfoximine (Msx), elicit responses grossly similar to those of limiting nitrogen, implicating both glutamine synthesis and TorC1 in the regulation of Gln3 and Gat1. To better understand this regulation, we compared Msx- versus Rap-elicited Gln3 and Gat1 localization, their DNA binding, nitrogen catabolite repression-sensitive gene expression, and the TorC1 pathway phosphatase requirements for these responses. Using this information we queried whether Rap and Msx inhibit sequential steps in a single, linear cascade connecting glutamine availability to Gln3 and Gat1 control as currently accepted or alternatively inhibit steps in two distinct parallel pathways. We find that Rap most strongly elicits nuclear Gat1 localization and expression of genes whose transcription is most Gat1-dependent. Msx, on the other hand, elicits nuclear Gln3 but not Gat1 localization and expression of genes that are most Gln3-dependent. Importantly, Rap-elicited nuclear Gln3 localization is absolutely Sit4-dependent, but that elicited by Msx is not. PP2A, although not always required for nuclear GATA factor localization, is highly required for GATA factor binding to nitrogen-responsive promoters and subsequent transcription irrespective of the gene GATA factor specificities. Collectively, our data support the existence of two different nitrogen-responsive regulatory pathways, one inhibited by Msx and the other by rapamycin.
DOI: 10.1074/jbc.M111.290577
PubMed: 22039046
PubMed Central: PMC3248002
Affiliations:
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TorC1 inhibitor, rapamycin (Rap), and glutamine synthetase inhibitor, methionine sulfoximine (Msx), elicit responses grossly similar to those of limiting nitrogen, implicating both glutamine synthesis and TorC1 in the regulation of Gln3 and Gat1. To better understand this regulation, we compared Msx- versus Rap-elicited Gln3 and Gat1 localization, their DNA binding, nitrogen catabolite repression-sensitive gene expression, and the TorC1 pathway phosphatase requirements for these responses. Using this information we queried whether Rap and Msx inhibit sequential steps in a single, linear cascade connecting glutamine availability to Gln3 and Gat1 control as currently accepted or alternatively inhibit steps in two distinct parallel pathways. We find that Rap most strongly elicits nuclear Gat1 localization and expression of genes whose transcription is most Gat1-dependent. Msx, on the other hand, elicits nuclear Gln3 but not Gat1 localization and expression of genes that are most Gln3-dependent. Importantly, Rap-elicited nuclear Gln3 localization is absolutely Sit4-dependent, but that elicited by Msx is not. PP2A, although not always required for nuclear GATA factor localization, is highly required for GATA factor binding to nitrogen-responsive promoters and subsequent transcription irrespective of the gene GATA factor specificities. Collectively, our data support the existence of two different nitrogen-responsive regulatory pathways, one inhibited by Msx and the other by rapamycin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22039046</PMID><DateCompleted><Year>2012</Year><Month>02</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>286</Volume><Issue>52</Issue><PubDate><Year>2011</Year><Month>Dec</Month><Day>30</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Nitrogen-responsive regulation of GATA protein family activators Gln3 and Gat1 occurs by two distinct pathways, one inhibited by rapamycin and the other by methionine sulfoximine.</ArticleTitle><Pagination><MedlinePgn>44897-912</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M111.290577</ELocationID><Abstract><AbstractText>Nitrogen availability regulates the transcription of genes required to degrade non-preferentially utilized nitrogen sources by governing the localization and function of transcription activators, Gln3 and Gat1. TorC1 inhibitor, rapamycin (Rap), and glutamine synthetase inhibitor, methionine sulfoximine (Msx), elicit responses grossly similar to those of limiting nitrogen, implicating both glutamine synthesis and TorC1 in the regulation of Gln3 and Gat1. To better understand this regulation, we compared Msx- versus Rap-elicited Gln3 and Gat1 localization, their DNA binding, nitrogen catabolite repression-sensitive gene expression, and the TorC1 pathway phosphatase requirements for these responses. Using this information we queried whether Rap and Msx inhibit sequential steps in a single, linear cascade connecting glutamine availability to Gln3 and Gat1 control as currently accepted or alternatively inhibit steps in two distinct parallel pathways. We find that Rap most strongly elicits nuclear Gat1 localization and expression of genes whose transcription is most Gat1-dependent. Msx, on the other hand, elicits nuclear Gln3 but not Gat1 localization and expression of genes that are most Gln3-dependent. Importantly, Rap-elicited nuclear Gln3 localization is absolutely Sit4-dependent, but that elicited by Msx is not. PP2A, although not always required for nuclear GATA factor localization, is highly required for GATA factor binding to nitrogen-responsive promoters and subsequent transcription irrespective of the gene GATA factor specificities. Collectively, our data support the existence of two different nitrogen-responsive regulatory pathways, one inhibited by Msx and the other by rapamycin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Georis</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Institut de Recherches Microbiologiques JM Wiame, Laboratoire de Microbiologie Université Libre de Bruxelles, B1070 Brussels, Belgium.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tate</LastName><ForeName>Jennifer J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Cooper</LastName><ForeName>Terrance G</ForeName><Initials>TG</Initials></Author><Author ValidYN="Y"><LastName>Dubois</LastName><ForeName>Evelyne</ForeName><Initials>E</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM035642</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>GM-35642</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>10</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000935">Antifungal Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C096100">GAT1 protein, S 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Fungal</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005973" MajorTopicYN="N">Glutamine</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008717" MajorTopicYN="N">Methionine Sulfoximine</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020218" MajorTopicYN="N">Response Elements</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName 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Cooper</name><name sortKey="Dubois, Evelyne" sort="Dubois, Evelyne" uniqKey="Dubois E" first="Evelyne" last="Dubois">Evelyne Dubois</name><name sortKey="Tate, Jennifer J" sort="Tate, Jennifer J" uniqKey="Tate J" first="Jennifer J" last="Tate">Jennifer J. Tate</name></noCountry><country name="Belgique"><noRegion><name sortKey="Georis, Isabelle" sort="Georis, Isabelle" uniqKey="Georis I" first="Isabelle" last="Georis">Isabelle Georis</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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