General Amino Acid Control and 14-3-3 Proteins Bmh1/2 Are Required for Nitrogen Catabolite Repression-Sensitive Regulation of Gln3 and Gat1 Localization.
Identifieur interne : 000839 ( Main/Exploration ); précédent : 000838; suivant : 000840General Amino Acid Control and 14-3-3 Proteins Bmh1/2 Are Required for Nitrogen Catabolite Repression-Sensitive Regulation of Gln3 and Gat1 Localization.
Auteurs : Jennifer J. Tate [États-Unis] ; David Buford [États-Unis] ; Rajendra Rai [États-Unis] ; Terrance G. Cooper [États-Unis]Source :
- Genetics [ 1943-2631 ] ; 2017.
Descripteurs français
- KwdFr :
- Acides aminés (métabolisme), Azote (métabolisme), Complexe-1 cible mécanistique de la rapamycine (MeSH), Complexes multiprotéiques (génétique), Complexes multiprotéiques (métabolisme), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Facteurs de transcription GATA (génétique), Facteurs de transcription GATA (métabolisme), Facteurs de transcription à motif basique et à glissière à leucines (génétique), Facteurs de transcription à motif basique et à glissière à leucines (métabolisme), Glutathione peroxidase (génétique), Glutathione peroxidase (métabolisme), Maturation post-traductionnelle des protéines (MeSH), Noyau de la cellule (métabolisme), Phosphorylation (MeSH), Prions (génétique), Prions (métabolisme), Protein-Serine-Threonine Kinases (génétique), Protein-Serine-Threonine Kinases (métabolisme), Protéines 14-3-3 (génétique), Protéines 14-3-3 (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Répression catabolique (MeSH), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Sérine-thréonine kinases TOR (génétique), Sérine-thréonine kinases TOR (métabolisme), Transport nucléaire actif (MeSH), Épistasie (MeSH).
- MESH :
- génétique : Complexes multiprotéiques, Facteurs de transcription, Facteurs de transcription GATA, Facteurs de transcription à motif basique et à glissière à leucines, Glutathione peroxidase, Prions, Protein-Serine-Threonine Kinases, Protéines 14-3-3, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- métabolisme : Acides aminés, Azote, Complexes multiprotéiques, Facteurs de transcription, Facteurs de transcription GATA, Facteurs de transcription à motif basique et à glissière à leucines, Glutathione peroxidase, Noyau de la cellule, Prions, Protein-Serine-Threonine Kinases, Protéines 14-3-3, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae, Sérine-thréonine kinases TOR.
- Complexe-1 cible mécanistique de la rapamycine, Maturation post-traductionnelle des protéines, Phosphorylation, Répression catabolique, Transport nucléaire actif, Épistasie.
English descriptors
- KwdEn :
- 14-3-3 Proteins (genetics), 14-3-3 Proteins (metabolism), Active Transport, Cell Nucleus (MeSH), Amino Acids (metabolism), Basic-Leucine Zipper Transcription Factors (genetics), Basic-Leucine Zipper Transcription Factors (metabolism), Catabolite Repression (MeSH), Cell Nucleus (metabolism), Epistasis, Genetic (MeSH), GATA Transcription Factors (genetics), GATA Transcription Factors (metabolism), Glutathione Peroxidase (genetics), Glutathione Peroxidase (metabolism), Mechanistic Target of Rapamycin Complex 1 (MeSH), Multiprotein Complexes (genetics), Multiprotein Complexes (metabolism), Nitrogen (metabolism), Phosphorylation (MeSH), Prions (genetics), Prions (metabolism), Protein Processing, Post-Translational (MeSH), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), TOR Serine-Threonine Kinases (genetics), TOR Serine-Threonine Kinases (metabolism), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : 14-3-3 Proteins, Basic-Leucine Zipper Transcription Factors, GATA Transcription Factors, Glutathione Peroxidase, Multiprotein Complexes, Prions, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors.
- chemical , metabolism : 14-3-3 Proteins, Amino Acids, Basic-Leucine Zipper Transcription Factors, GATA Transcription Factors, Glutathione Peroxidase, Multiprotein Complexes, Nitrogen, Prions, Protein-Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, TOR Serine-Threonine Kinases, Transcription Factors.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, Saccharomyces cerevisiae.
- Active Transport, Cell Nucleus, Catabolite Repression, Epistasis, Genetic, Mechanistic Target of Rapamycin Complex 1, Phosphorylation, Protein Processing, Post-Translational.
Abstract
Nitrogen catabolite repression (NCR), the ability of Saccharomyces cerevisiae to use good nitrogen sources in preference to poor ones, derives from nitrogen-responsive regulation of the GATA family transcription activators Gln3 and Gat1 In nitrogen-replete conditions, the GATA factors are cytoplasmic and NCR-sensitive transcription minimal. When only poor nitrogen sources are available, Gln3 is nuclear, dramatically increasing GATA factor-mediated transcription. This regulation was originally attributed to mechanistic Tor protein kinase complex 1 (mTorC1)-mediated control of Gln3 However, we recently showed that two regulatory systems act cumulatively to maintain cytoplasmic Gln3 sequestration, only one of which is mTorC1. Present experiments demonstrate that the other previously elusive component is uncharged transfer RNA-activated, Gcn2 protein kinase-mediated general amino acid control (GAAC). Gcn2 and Gcn4 are required for NCR-sensitive nuclear Gln3-Myc13 localization, and from epistasis experiments Gcn2 appears to function upstream of Ure2 Bmh1/2 are also required for nuclear Gln3-Myc13 localization and appear to function downstream of Ure2 Overall, Gln3 phosphorylation levels decrease upon loss of Gcn2, Gcn4, or Bmh1/2 Our results add a new dimension to nitrogen-responsive GATA-factor regulation and demonstrate the cumulative participation of the mTorC1 and GAAC pathways, which respond oppositely to nitrogen availability, in the nitrogen-responsive control of catabolic gene expression in yeast.
DOI: 10.1534/genetics.116.195800
PubMed: 28007891
PubMed Central: PMC5289842
Affiliations:
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Tate</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Tennessee</region></placeName><wicri:cityArea>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis</wicri:cityArea></affiliation></author><author><name sortKey="Buford, David" sort="Buford, David" uniqKey="Buford D" first="David" last="Buford">David Buford</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Tennessee</region></placeName><wicri:cityArea>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis</wicri:cityArea></affiliation></author><author><name sortKey="Rai, Rajendra" sort="Rai, Rajendra" uniqKey="Rai R" first="Rajendra" last="Rai">Rajendra Rai</name><affiliation wicri:level="2"><nlm:affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Tennessee</region></placeName><wicri:cityArea>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis</wicri:cityArea></affiliation></author><author><name sortKey="Cooper, Terrance G" sort="Cooper, Terrance G" uniqKey="Cooper T" first="Terrance G" last="Cooper">Terrance G. Cooper</name><affiliation wicri:level="1"><nlm:affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163 tcooper@uthsc.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis</wicri:regionArea><wicri:noRegion>Memphis</wicri:noRegion></affiliation></author></analytic><series><title level="j">Genetics</title><idno type="eISSN">1943-2631</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>14-3-3 Proteins (genetics)</term><term>14-3-3 Proteins (metabolism)</term><term>Active Transport, Cell Nucleus (MeSH)</term><term>Amino Acids (metabolism)</term><term>Basic-Leucine Zipper Transcription Factors (genetics)</term><term>Basic-Leucine Zipper Transcription Factors (metabolism)</term><term>Catabolite Repression (MeSH)</term><term>Cell Nucleus (metabolism)</term><term>Epistasis, Genetic (MeSH)</term><term>GATA Transcription Factors (genetics)</term><term>GATA Transcription Factors (metabolism)</term><term>Glutathione Peroxidase (genetics)</term><term>Glutathione Peroxidase (metabolism)</term><term>Mechanistic Target of Rapamycin Complex 1 (MeSH)</term><term>Multiprotein Complexes (genetics)</term><term>Multiprotein Complexes (metabolism)</term><term>Nitrogen (metabolism)</term><term>Phosphorylation (MeSH)</term><term>Prions (genetics)</term><term>Prions (metabolism)</term><term>Protein Processing, Post-Translational (MeSH)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>TOR Serine-Threonine Kinases (genetics)</term><term>TOR Serine-Threonine Kinases (metabolism)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés (métabolisme)</term><term>Azote (métabolisme)</term><term>Complexe-1 cible mécanistique de la rapamycine (MeSH)</term><term>Complexes multiprotéiques (génétique)</term><term>Complexes multiprotéiques (métabolisme)</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>Facteurs de transcription à motif basique et à glissière à leucines (génétique)</term><term>Facteurs de transcription à motif basique et à glissière à leucines (métabolisme)</term><term>Glutathione peroxidase (génétique)</term><term>Glutathione peroxidase (métabolisme)</term><term>Maturation post-traductionnelle des protéines (MeSH)</term><term>Noyau de la cellule (métabolisme)</term><term>Phosphorylation (MeSH)</term><term>Prions (génétique)</term><term>Prions (métabolisme)</term><term>Protein-Serine-Threonine Kinases (génétique)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines 14-3-3 (génétique)</term><term>Protéines 14-3-3 (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Répression catabolique (MeSH)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sérine-thréonine kinases TOR (génétique)</term><term>Sérine-thréonine kinases TOR (métabolisme)</term><term>Transport nucléaire actif (MeSH)</term><term>Épistasie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>14-3-3 Proteins</term><term>Basic-Leucine Zipper Transcription Factors</term><term>GATA Transcription Factors</term><term>Glutathione Peroxidase</term><term>Multiprotein Complexes</term><term>Prions</term><term>Protein-Serine-Threonine Kinases</term><term>Saccharomyces cerevisiae Proteins</term><term>TOR Serine-Threonine Kinases</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>14-3-3 Proteins</term><term>Amino Acids</term><term>Basic-Leucine Zipper Transcription Factors</term><term>GATA Transcription Factors</term><term>Glutathione Peroxidase</term><term>Multiprotein Complexes</term><term>Nitrogen</term><term>Prions</term><term>Protein-Serine-Threonine Kinases</term><term>Saccharomyces cerevisiae Proteins</term><term>TOR Serine-Threonine Kinases</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexes multiprotéiques</term><term>Facteurs de transcription</term><term>Facteurs de transcription GATA</term><term>Facteurs de transcription à motif basique et à glissière à leucines</term><term>Glutathione peroxidase</term><term>Prions</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines 14-3-3</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides aminés</term><term>Azote</term><term>Complexes multiprotéiques</term><term>Facteurs de transcription</term><term>Facteurs de transcription GATA</term><term>Facteurs de transcription à motif basique et à glissière à leucines</term><term>Glutathione peroxidase</term><term>Noyau de la cellule</term><term>Prions</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines 14-3-3</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Sérine-thréonine kinases TOR</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term><term>Catabolite Repression</term><term>Epistasis, Genetic</term><term>Mechanistic Target of Rapamycin Complex 1</term><term>Phosphorylation</term><term>Protein Processing, Post-Translational</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term><term>Maturation post-traductionnelle des protéines</term><term>Phosphorylation</term><term>Répression catabolique</term><term>Transport nucléaire actif</term><term>Épistasie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nitrogen catabolite repression (NCR), the ability of Saccharomyces cerevisiae to use good nitrogen sources in preference to poor ones, derives from nitrogen-responsive regulation of the GATA family transcription activators Gln3 and Gat1 In nitrogen-replete conditions, the GATA factors are cytoplasmic and NCR-sensitive transcription minimal. When only poor nitrogen sources are available, Gln3 is nuclear, dramatically increasing GATA factor-mediated transcription. This regulation was originally attributed to mechanistic Tor protein kinase complex 1 (mTorC1)-mediated control of Gln3 However, we recently showed that two regulatory systems act cumulatively to maintain cytoplasmic Gln3 sequestration, only one of which is mTorC1. Present experiments demonstrate that the other previously elusive component is uncharged transfer RNA-activated, Gcn2 protein kinase-mediated general amino acid control (GAAC). Gcn2 and Gcn4 are required for NCR-sensitive nuclear Gln3-Myc<sup>13</sup> localization, and from epistasis experiments Gcn2 appears to function upstream of Ure2 Bmh1/2 are also required for nuclear Gln3-Myc<sup>13</sup> localization and appear to function downstream of Ure2 Overall, Gln3 phosphorylation levels decrease upon loss of Gcn2, Gcn4, or Bmh1/2 Our results add a new dimension to nitrogen-responsive GATA-factor regulation and demonstrate the cumulative participation of the mTorC1 and GAAC pathways, which respond oppositely to nitrogen availability, in the nitrogen-responsive control of catabolic gene expression in yeast.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28007891</PMID><DateCompleted><Year>2017</Year><Month>05</Month><Day>30</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1943-2631</ISSN><JournalIssue CitedMedium="Internet"><Volume>205</Volume><Issue>2</Issue><PubDate><Year>2017</Year><Month>02</Month></PubDate></JournalIssue><Title>Genetics</Title><ISOAbbreviation>Genetics</ISOAbbreviation></Journal><ArticleTitle>General Amino Acid Control and 14-3-3 Proteins Bmh1/2 Are Required for Nitrogen Catabolite Repression-Sensitive Regulation of Gln3 and Gat1 Localization.</ArticleTitle><Pagination><MedlinePgn>633-655</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1534/genetics.116.195800</ELocationID><Abstract><AbstractText>Nitrogen catabolite repression (NCR), the ability of Saccharomyces cerevisiae to use good nitrogen sources in preference to poor ones, derives from nitrogen-responsive regulation of the GATA family transcription activators Gln3 and Gat1 In nitrogen-replete conditions, the GATA factors are cytoplasmic and NCR-sensitive transcription minimal. When only poor nitrogen sources are available, Gln3 is nuclear, dramatically increasing GATA factor-mediated transcription. This regulation was originally attributed to mechanistic Tor protein kinase complex 1 (mTorC1)-mediated control of Gln3 However, we recently showed that two regulatory systems act cumulatively to maintain cytoplasmic Gln3 sequestration, only one of which is mTorC1. Present experiments demonstrate that the other previously elusive component is uncharged transfer RNA-activated, Gcn2 protein kinase-mediated general amino acid control (GAAC). Gcn2 and Gcn4 are required for NCR-sensitive nuclear Gln3-Myc<sup>13</sup> localization, and from epistasis experiments Gcn2 appears to function upstream of Ure2 Bmh1/2 are also required for nuclear Gln3-Myc<sup>13</sup> localization and appear to function downstream of Ure2 Overall, Gln3 phosphorylation levels decrease upon loss of Gcn2, Gcn4, or Bmh1/2 Our results add a new dimension to nitrogen-responsive GATA-factor regulation and demonstrate the cumulative participation of the mTorC1 and GAAC pathways, which respond oppositely to nitrogen availability, in the nitrogen-responsive control of catabolic gene expression in yeast.</AbstractText><CopyrightInformation>Copyright © 2017 by the Genetics Society of America.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tate</LastName><ForeName>Jennifer J</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Buford</LastName><ForeName>David</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rai</LastName><ForeName>Rajendra</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cooper</LastName><ForeName>Terrance G</ForeName><Initials>TG</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Immunology, and Biochemistry, University of Tennessee Health Science Center, Memphis, Tennessee 38163 tcooper@uthsc.edu.</Affiliation></AffiliationInfo></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></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>12</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Genetics</MedlineTA><NlmUniqueID>0374636</NlmUniqueID><ISSNLinking>0016-6731</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048948">14-3-3 Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000596">Amino Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050976">Basic-Leucine Zipper Transcription Factors</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="C501391">GCN4 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C071664">GLN3 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046912">Multiprotein Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011328">Prions</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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