Intranuclear function for protein phosphatase 2A: Pph21 and Pph22 are required for rapamycin-induced GATA factor binding to the DAL5 promoter in yeast.
Identifieur interne : 001302 ( Main/Exploration ); précédent : 001301; suivant : 001303Intranuclear function for protein phosphatase 2A: Pph21 and Pph22 are required for rapamycin-induced GATA factor binding to the DAL5 promoter in yeast.
Auteurs : Isabelle Georis [Belgique] ; Jennifer J. Tate ; André Feller ; Terrance G. Cooper ; Evelyne DuboisSource :
- Molecular and cellular biology [ 1098-5549 ] ; 2011.
Descripteurs français
- KwdFr :
- Amorces ADN (génétique), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Facteurs de transcription GATA (génétique), Facteurs de transcription GATA (métabolisme), Glutathione peroxidase (génétique), Glutathione peroxidase (métabolisme), Gènes fongiques (MeSH), Mutation (MeSH), Noyau de la cellule (métabolisme), Prions (génétique), Prions (métabolisme), Protein Phosphatase 2 (génétique), Protein Phosphatase 2 (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines de fusion recombinantes (génétique), Protéines de fusion recombinantes (métabolisme), Protéines de transport membranaire (génétique), Protéines mutantes (génétique), Protéines mutantes (métabolisme), Protéines à fluorescence verte (génétique), Protéines à fluorescence verte (métabolisme), Régions promotrices (génétique) (MeSH), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Sites de fixation (génétique), Séquence nucléotidique (MeSH), Transduction du signal (MeSH).
- MESH :
- effets des médicaments et des substances chimiques : Saccharomyces cerevisiae.
- génétique : Amorces ADN, Facteurs de transcription, Facteurs de transcription GATA, Glutathione peroxidase, Prions, Protein Phosphatase 2, Protéines de Saccharomyces cerevisiae, Protéines de fusion recombinantes, Protéines de transport membranaire, Protéines mutantes, Protéines à fluorescence verte, Saccharomyces cerevisiae, Sites de fixation.
- métabolisme : Facteurs de transcription, Facteurs de transcription GATA, Glutathione peroxidase, Noyau de la cellule, Prions, Protein Phosphatase 2, Protéines de Saccharomyces cerevisiae, Protéines de fusion recombinantes, Protéines mutantes, Protéines à fluorescence verte, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- Gènes fongiques, Mutation, Régions promotrices (génétique), Séquence nucléotidique, Transduction du signal.
English descriptors
- KwdEn :
- Base Sequence (MeSH), Binding Sites (genetics), Cell Nucleus (metabolism), DNA Primers (genetics), GATA Transcription Factors (genetics), GATA Transcription Factors (metabolism), Genes, Fungal (MeSH), Glutathione Peroxidase (genetics), Glutathione Peroxidase (metabolism), Green Fluorescent Proteins (genetics), Green Fluorescent Proteins (metabolism), Membrane Transport Proteins (genetics), Mutant Proteins (genetics), Mutant Proteins (metabolism), Mutation (MeSH), Prions (genetics), Prions (metabolism), Promoter Regions, Genetic (MeSH), Protein Phosphatase 2 (genetics), Protein Phosphatase 2 (metabolism), Recombinant Fusion Proteins (genetics), Recombinant Fusion Proteins (metabolism), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Signal Transduction (MeSH), Sirolimus (pharmacology), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : DNA Primers, GATA Transcription Factors, Glutathione Peroxidase, Green Fluorescent Proteins, Membrane Transport Proteins, Mutant Proteins, Prions, Protein Phosphatase 2, Recombinant Fusion Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors.
- drug effects : Saccharomyces cerevisiae.
- genetics : Binding Sites, Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, GATA Transcription Factors, Glutathione Peroxidase, Green Fluorescent Proteins, Mutant Proteins, Prions, Protein Phosphatase 2, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Sirolimus.
- Base Sequence, Genes, Fungal, Mutation, Promoter Regions, Genetic, Signal Transduction.
Abstract
Protein phosphatase 2A (PP2A), a central Tor pathway phosphatase consisting of a catalytic subunit (Pph21 or Pph22), a scaffold subunit (Tpd3), and one of two regulatory subunits (Cdc55 or Rts1), has been repeatedly shown to play important roles in cytoplasmically localized signal transduction activities. In contrast, its involvement in intranuclear control of mRNA production has heretofore not been reported. Here, we demonstrate for the first time that binding of the nitrogen catabolite repression-responsive GATA transcription activators (Gln3 and Gat1) to the DAL5 promoter and DAL5 expression require Pph21/22-Tpd3-Cdc55/Rts1 in rapamycin-treated glutamine-grown cells. This conclusion is supported by the following observations. (i) Rapamycin-induced DAL5 expression along with Gln3 and Gat1 binding to the DAL5 promoter fails to occur in pph21Δ pph22Δ, tpd3Δ, and cdc55Δ rts1Δ mutants. (ii) The Pph21/22 requirement persists even when Gat1 and Gln3 are rendered constitutively nuclear, thus dissociating the intranuclear requirement of PP2A from its partial requirement for rapamycin-induced nuclear Gat1 localization. (iii) Pph21-Myc(13) (Ppp21 tagged at the C terminus with 13 copies of the Myc epitope) weakly associates with the DAL5 promoter in a Gat1-dependent manner, whereas a similar Pph22-Myc(13) association requires both Gln3 and Gat1. Finally, we demonstrate that a pph21Δ pph22Δ double mutant is epistatic to ure2Δ for nuclear Gat1 localization in untreated glutamine-grown cells, whereas for Gln3, just the opposite occurs: i.e., ure2Δ is epistatic to pph21Δ pph22Δ. This final observation adds additional support to our previous conclusion that the Gln3 and Gat1 GATA factor localizations are predominantly controlled by different regulatory pathways.
DOI: 10.1128/MCB.00482-10
PubMed: 20974806
PubMed Central: PMC3019842
Affiliations:
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Wiame, Laboratoire de Microbiologie, Université Libre de Bruxelles, B1070 Brussels, Belgium.</nlm:affiliation><country xml:lang="fr">Belgique</country><wicri:regionArea>Institut de Recherches Microbiologiques J.-M. Wiame, Laboratoire de Microbiologie, Université Libre de Bruxelles, B1070 Brussels</wicri:regionArea><orgName type="university">Université libre de Bruxelles</orgName><placeName><settlement type="city">Bruxelles</settlement><region type="region" nuts="2">Région de Bruxelles-Capitale</region></placeName></affiliation></author><author><name sortKey="Tate, Jennifer J" sort="Tate, Jennifer J" uniqKey="Tate J" first="Jennifer J" last="Tate">Jennifer J. Tate</name></author><author><name sortKey="Feller, Andre" sort="Feller, Andre" uniqKey="Feller A" first="André" last="Feller">André Feller</name></author><author><name sortKey="Cooper, Terrance G" sort="Cooper, Terrance G" uniqKey="Cooper T" first="Terrance G" last="Cooper">Terrance G. Cooper</name></author><author><name sortKey="Dubois, Evelyne" sort="Dubois, Evelyne" uniqKey="Dubois E" first="Evelyne" last="Dubois">Evelyne Dubois</name></author></analytic><series><title level="j">Molecular and cellular biology</title><idno type="eISSN">1098-5549</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>Binding Sites (genetics)</term><term>Cell Nucleus (metabolism)</term><term>DNA Primers (genetics)</term><term>GATA Transcription Factors (genetics)</term><term>GATA Transcription Factors (metabolism)</term><term>Genes, Fungal (MeSH)</term><term>Glutathione Peroxidase (genetics)</term><term>Glutathione Peroxidase (metabolism)</term><term>Green Fluorescent Proteins (genetics)</term><term>Green Fluorescent Proteins (metabolism)</term><term>Membrane Transport Proteins (genetics)</term><term>Mutant Proteins (genetics)</term><term>Mutant Proteins (metabolism)</term><term>Mutation (MeSH)</term><term>Prions (genetics)</term><term>Prions (metabolism)</term><term>Promoter Regions, Genetic (MeSH)</term><term>Protein Phosphatase 2 (genetics)</term><term>Protein Phosphatase 2 (metabolism)</term><term>Recombinant Fusion Proteins (genetics)</term><term>Recombinant Fusion Proteins (metabolism)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Sirolimus (pharmacology)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN (génétique)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Facteurs de transcription GATA (génétique)</term><term>Facteurs de transcription GATA (métabolisme)</term><term>Glutathione peroxidase (génétique)</term><term>Glutathione peroxidase (métabolisme)</term><term>Gènes fongiques (MeSH)</term><term>Mutation (MeSH)</term><term>Noyau de la cellule (métabolisme)</term><term>Prions (génétique)</term><term>Prions (métabolisme)</term><term>Protein Phosphatase 2 (génétique)</term><term>Protein Phosphatase 2 (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Protéines de fusion recombinantes (génétique)</term><term>Protéines de fusion recombinantes (métabolisme)</term><term>Protéines de transport membranaire (génétique)</term><term>Protéines mutantes (génétique)</term><term>Protéines mutantes (métabolisme)</term><term>Protéines à fluorescence verte (génétique)</term><term>Protéines à fluorescence verte (métabolisme)</term><term>Régions promotrices (génétique) (MeSH)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Sites de fixation (génétique)</term><term>Séquence nucléotidique (MeSH)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA Primers</term><term>GATA Transcription Factors</term><term>Glutathione Peroxidase</term><term>Green Fluorescent Proteins</term><term>Membrane Transport Proteins</term><term>Mutant Proteins</term><term>Prions</term><term>Protein Phosphatase 2</term><term>Recombinant Fusion Proteins</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Amorces ADN</term><term>Facteurs de transcription</term><term>Facteurs de transcription GATA</term><term>Glutathione peroxidase</term><term>Prions</term><term>Protein Phosphatase 2</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de fusion recombinantes</term><term>Protéines de transport membranaire</term><term>Protéines mutantes</term><term>Protéines à fluorescence verte</term><term>Saccharomyces cerevisiae</term><term>Sites de fixation</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>GATA Transcription Factors</term><term>Glutathione Peroxidase</term><term>Green Fluorescent Proteins</term><term>Mutant Proteins</term><term>Prions</term><term>Protein Phosphatase 2</term><term>Recombinant Fusion Proteins</term><term>Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de transcription</term><term>Facteurs de transcription GATA</term><term>Glutathione peroxidase</term><term>Noyau de la cellule</term><term>Prions</term><term>Protein Phosphatase 2</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines de fusion recombinantes</term><term>Protéines mutantes</term><term>Protéines à fluorescence verte</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Genes, Fungal</term><term>Mutation</term><term>Promoter Regions, Genetic</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Gènes fongiques</term><term>Mutation</term><term>Régions promotrices (génétique)</term><term>Séquence nucléotidique</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Protein phosphatase 2A (PP2A), a central Tor pathway phosphatase consisting of a catalytic subunit (Pph21 or Pph22), a scaffold subunit (Tpd3), and one of two regulatory subunits (Cdc55 or Rts1), has been repeatedly shown to play important roles in cytoplasmically localized signal transduction activities. In contrast, its involvement in intranuclear control of mRNA production has heretofore not been reported. Here, we demonstrate for the first time that binding of the nitrogen catabolite repression-responsive GATA transcription activators (Gln3 and Gat1) to the DAL5 promoter and DAL5 expression require Pph21/22-Tpd3-Cdc55/Rts1 in rapamycin-treated glutamine-grown cells. This conclusion is supported by the following observations. (i) Rapamycin-induced DAL5 expression along with Gln3 and Gat1 binding to the DAL5 promoter fails to occur in pph21Δ pph22Δ, tpd3Δ, and cdc55Δ rts1Δ mutants. (ii) The Pph21/22 requirement persists even when Gat1 and Gln3 are rendered constitutively nuclear, thus dissociating the intranuclear requirement of PP2A from its partial requirement for rapamycin-induced nuclear Gat1 localization. (iii) Pph21-Myc(13) (Ppp21 tagged at the C terminus with 13 copies of the Myc epitope) weakly associates with the DAL5 promoter in a Gat1-dependent manner, whereas a similar Pph22-Myc(13) association requires both Gln3 and Gat1. Finally, we demonstrate that a pph21Δ pph22Δ double mutant is epistatic to ure2Δ for nuclear Gat1 localization in untreated glutamine-grown cells, whereas for Gln3, just the opposite occurs: i.e., ure2Δ is epistatic to pph21Δ pph22Δ. This final observation adds additional support to our previous conclusion that the Gln3 and Gat1 GATA factor localizations are predominantly controlled by different regulatory pathways.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20974806</PMID><DateCompleted><Year>2011</Year><Month>01</Month><Day>27</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5549</ISSN><JournalIssue CitedMedium="Internet"><Volume>31</Volume><Issue>1</Issue><PubDate><Year>2011</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Intranuclear function for protein phosphatase 2A: Pph21 and Pph22 are required for rapamycin-induced GATA factor binding to the DAL5 promoter in yeast.</ArticleTitle><Pagination><MedlinePgn>92-104</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/MCB.00482-10</ELocationID><Abstract><AbstractText>Protein phosphatase 2A (PP2A), a central Tor pathway phosphatase consisting of a catalytic subunit (Pph21 or Pph22), a scaffold subunit (Tpd3), and one of two regulatory subunits (Cdc55 or Rts1), has been repeatedly shown to play important roles in cytoplasmically localized signal transduction activities. In contrast, its involvement in intranuclear control of mRNA production has heretofore not been reported. Here, we demonstrate for the first time that binding of the nitrogen catabolite repression-responsive GATA transcription activators (Gln3 and Gat1) to the DAL5 promoter and DAL5 expression require Pph21/22-Tpd3-Cdc55/Rts1 in rapamycin-treated glutamine-grown cells. This conclusion is supported by the following observations. (i) Rapamycin-induced DAL5 expression along with Gln3 and Gat1 binding to the DAL5 promoter fails to occur in pph21Δ pph22Δ, tpd3Δ, and cdc55Δ rts1Δ mutants. (ii) The Pph21/22 requirement persists even when Gat1 and Gln3 are rendered constitutively nuclear, thus dissociating the intranuclear requirement of PP2A from its partial requirement for rapamycin-induced nuclear Gat1 localization. (iii) Pph21-Myc(13) (Ppp21 tagged at the C terminus with 13 copies of the Myc epitope) weakly associates with the DAL5 promoter in a Gat1-dependent manner, whereas a similar Pph22-Myc(13) association requires both Gln3 and Gat1. Finally, we demonstrate that a pph21Δ pph22Δ double mutant is epistatic to ure2Δ for nuclear Gat1 localization in untreated glutamine-grown cells, whereas for Gln3, just the opposite occurs: i.e., ure2Δ is epistatic to pph21Δ pph22Δ. This final observation adds additional support to our previous conclusion that the Gln3 and Gat1 GATA factor localizations are predominantly controlled by different regulatory pathways.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Georis</LastName><ForeName>Isabelle</ForeName><Initials>I</Initials><AffiliationInfo><Affiliation>Institut de Recherches Microbiologiques J.-M. 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>Feller</LastName><ForeName>André</ForeName><Initials>A</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>R01 GM035642-22</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>2010</Year><Month>10</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Biol</MedlineTA><NlmUniqueID>8109087</NlmUniqueID><ISSNLinking>0270-7306</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C503299">DAL5 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C096100">GAT1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050980">GATA Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026901">Membrane Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050505">Mutant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011993">Recombinant Fusion 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>147336-22-9</RegistryNumber><NameOfSubstance UI="D049452">Green Fluorescent Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="D005979">Glutathione Peroxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.9</RegistryNumber><NameOfSubstance UI="C067020">URE2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="C483105">PPH21 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="C465217">Pph22 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D054648">Protein Phosphatase 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>W36ZG6FT64</RegistryNumber><NameOfSubstance UI="D020123">Sirolimus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050980" MajorTopicYN="N">GATA Transcription Factors</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" 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