Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.
Identifieur interne : 001086 ( Main/Exploration ); précédent : 001085; suivant : 001087Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.
Auteurs : S. Izawa [Japon] ; K. Maeda ; K. Sugiyama ; J. Mano ; Y. Inoue ; A. KimuraSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1999.
Descripteurs français
- KwdFr :
- Amorces ADN (MeSH), Facteurs de transcription (métabolisme), Glutarédoxines (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Protéines (métabolisme), Protéines de Saccharomyces cerevisiae (MeSH), Protéines de liaison à l'ADN (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Séquence nucléotidique (MeSH), Thiorédoxines (génétique), Thiorédoxines (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Base Sequence (MeSH), DNA Primers (MeSH), DNA-Binding Proteins (metabolism), Glutaredoxins (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Proteins (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (MeSH), Thioredoxins (genetics), Thioredoxins (metabolism), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : Thioredoxins.
- chemical , metabolism : DNA-Binding Proteins, Proteins, Thioredoxins, Transcription Factors.
- chemical : DNA Primers, Glutaredoxins, Oxidoreductases, Saccharomyces cerevisiae Proteins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Base Sequence, Mutation.
Abstract
Yap1 is a transcription factor that responds to oxidative stress in Saccharomyces cerevisiae. The activity of Yap1 is regulated at the level of its intracellular localization, and a cysteine-rich domain at the C terminus of Yap1 is involved in this regulation. We investigated the effects of redox-regulatory proteins, thioredoxin and glutaredoxin, on the regulation of Yap1, using the deficient mutants of these thiol-disulfide oxidoreductases. In the thioredoxin-deficient mutant (trx1Delta/trx2Delta), Yap1 was constitutively concentrated in the nucleus and the level of expression of the Yap1 target genes was high under normal conditions, while this was not the case for the glutaredoxin-deficient mutant (grx1Delta/grx2Delta). No distinct difference was observed in the levels of Yap1 protein between the wild type and trx1Delta/trx2Delta. The constitutive activation of Yap1 in trxDelta/trx2Delta was observed under aerobic conditions but not under anaerobic conditions. These findings suggest that thioredoxin has negative effects on this regulation via the redox states. We also show the synthetic lethality between yap1Delta and trx1Delta/trx2Delta mutation, but the yap1Delta/grx1Delta/grx2Delta triple mutant was viable, suggesting a difference of the functions between thioredoxin and glutaredoxin and a genetic interaction between Yap1 and thioredoxin in vivo.
DOI: 10.1074/jbc.274.40.28459
PubMed: 10497208
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.</title><author><name sortKey="Izawa, S" sort="Izawa, S" uniqKey="Izawa S" first="S" last="Izawa">S. Izawa</name><affiliation wicri:level="4"><nlm:affiliation>Department of Molecular Breeding of Microorganisms, Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Molecular Breeding of Microorganisms, Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011</wicri:regionArea><orgName type="university">Université de Kyoto</orgName><placeName><settlement type="city">Kyoto</settlement><region type="prefecture">Région du Kansai</region></placeName></affiliation></author><author><name sortKey="Maeda, K" sort="Maeda, K" uniqKey="Maeda K" first="K" last="Maeda">K. Maeda</name></author><author><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K" last="Sugiyama">K. Sugiyama</name></author><author><name sortKey="Mano, J" sort="Mano, J" uniqKey="Mano J" first="J" last="Mano">J. Mano</name></author><author><name sortKey="Inoue, Y" sort="Inoue, Y" uniqKey="Inoue Y" first="Y" last="Inoue">Y. Inoue</name></author><author><name sortKey="Kimura, A" sort="Kimura, A" uniqKey="Kimura A" first="A" last="Kimura">A. Kimura</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10497208</idno><idno type="pmid">10497208</idno><idno type="doi">10.1074/jbc.274.40.28459</idno><idno type="wicri:Area/Main/Corpus">001097</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001097</idno><idno type="wicri:Area/Main/Curation">001097</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001097</idno><idno type="wicri:Area/Main/Exploration">001097</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.</title><author><name sortKey="Izawa, S" sort="Izawa, S" uniqKey="Izawa S" first="S" last="Izawa">S. Izawa</name><affiliation wicri:level="4"><nlm:affiliation>Department of Molecular Breeding of Microorganisms, Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Molecular Breeding of Microorganisms, Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011</wicri:regionArea><orgName type="university">Université de Kyoto</orgName><placeName><settlement type="city">Kyoto</settlement><region type="prefecture">Région du Kansai</region></placeName></affiliation></author><author><name sortKey="Maeda, K" sort="Maeda, K" uniqKey="Maeda K" first="K" last="Maeda">K. Maeda</name></author><author><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K" last="Sugiyama">K. Sugiyama</name></author><author><name sortKey="Mano, J" sort="Mano, J" uniqKey="Mano J" first="J" last="Mano">J. Mano</name></author><author><name sortKey="Inoue, Y" sort="Inoue, Y" uniqKey="Inoue Y" first="Y" last="Inoue">Y. Inoue</name></author><author><name sortKey="Kimura, A" sort="Kimura, A" uniqKey="Kimura A" first="A" last="Kimura">A. Kimura</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Base Sequence (MeSH)</term><term>DNA Primers (MeSH)</term><term>DNA-Binding Proteins (metabolism)</term><term>Glutaredoxins (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (MeSH)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Amorces ADN (MeSH)</term><term>Facteurs de transcription (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (MeSH)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Séquence nucléotidique (MeSH)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA-Binding Proteins</term><term>Proteins</term><term>Thioredoxins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA Primers</term><term>Glutaredoxins</term><term>Oxidoreductases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Saccharomyces cerevisiae</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteurs de transcription</term><term>Protéines</term><term>Protéines de liaison à l'ADN</term><term>Saccharomyces cerevisiae</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Base Sequence</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Amorces ADN</term><term>Glutarédoxines</term><term>Mutation</term><term>Oxidoreductases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Yap1 is a transcription factor that responds to oxidative stress in Saccharomyces cerevisiae. The activity of Yap1 is regulated at the level of its intracellular localization, and a cysteine-rich domain at the C terminus of Yap1 is involved in this regulation. We investigated the effects of redox-regulatory proteins, thioredoxin and glutaredoxin, on the regulation of Yap1, using the deficient mutants of these thiol-disulfide oxidoreductases. In the thioredoxin-deficient mutant (trx1Delta/trx2Delta), Yap1 was constitutively concentrated in the nucleus and the level of expression of the Yap1 target genes was high under normal conditions, while this was not the case for the glutaredoxin-deficient mutant (grx1Delta/grx2Delta). No distinct difference was observed in the levels of Yap1 protein between the wild type and trx1Delta/trx2Delta. The constitutive activation of Yap1 in trxDelta/trx2Delta was observed under aerobic conditions but not under anaerobic conditions. These findings suggest that thioredoxin has negative effects on this regulation via the redox states. We also show the synthetic lethality between yap1Delta and trx1Delta/trx2Delta mutation, but the yap1Delta/grx1Delta/grx2Delta triple mutant was viable, suggesting a difference of the functions between thioredoxin and glutaredoxin and a genetic interaction between Yap1 and thioredoxin in vivo.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10497208</PMID><DateCompleted><Year>1999</Year><Month>11</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>274</Volume><Issue>40</Issue><PubDate><Year>1999</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>28459-65</MedlinePgn></Pagination><Abstract><AbstractText>Yap1 is a transcription factor that responds to oxidative stress in Saccharomyces cerevisiae. The activity of Yap1 is regulated at the level of its intracellular localization, and a cysteine-rich domain at the C terminus of Yap1 is involved in this regulation. We investigated the effects of redox-regulatory proteins, thioredoxin and glutaredoxin, on the regulation of Yap1, using the deficient mutants of these thiol-disulfide oxidoreductases. In the thioredoxin-deficient mutant (trx1Delta/trx2Delta), Yap1 was constitutively concentrated in the nucleus and the level of expression of the Yap1 target genes was high under normal conditions, while this was not the case for the glutaredoxin-deficient mutant (grx1Delta/grx2Delta). No distinct difference was observed in the levels of Yap1 protein between the wild type and trx1Delta/trx2Delta. The constitutive activation of Yap1 in trxDelta/trx2Delta was observed under aerobic conditions but not under anaerobic conditions. These findings suggest that thioredoxin has negative effects on this regulation via the redox states. We also show the synthetic lethality between yap1Delta and trx1Delta/trx2Delta mutation, but the yap1Delta/grx1Delta/grx2Delta triple mutant was viable, suggesting a difference of the functions between thioredoxin and glutaredoxin and a genetic interaction between Yap1 and thioredoxin in vivo.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Izawa</LastName><ForeName>S</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Molecular Breeding of Microorganisms, Research Institute for Food Science, Kyoto University, Uji, Kyoto 611-0011, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maeda</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Sugiyama</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Mano</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Inoue</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Kimura</LastName><ForeName>A</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></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="D017931">DNA Primers</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004268">DNA-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">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>0</RegistryNumber><NameOfSubstance UI="C086677">YAP1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</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 UI="D029701" MajorTopicYN="Y">Saccharomyces cerevisiae Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014157" MajorTopicYN="N">Transcription Factors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>9</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>9</Month><Day>25</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>9</Month><Day>25</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10497208</ArticleId><ArticleId IdType="doi">10.1074/jbc.274.40.28459</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country><region><li>Région du Kansai</li></region><settlement><li>Kyoto</li></settlement><orgName><li>Université de Kyoto</li></orgName></list><tree><noCountry><name sortKey="Inoue, Y" sort="Inoue, Y" uniqKey="Inoue Y" first="Y" last="Inoue">Y. Inoue</name><name sortKey="Kimura, A" sort="Kimura, A" uniqKey="Kimura A" first="A" last="Kimura">A. Kimura</name><name sortKey="Maeda, K" sort="Maeda, K" uniqKey="Maeda K" first="K" last="Maeda">K. Maeda</name><name sortKey="Mano, J" sort="Mano, J" uniqKey="Mano J" first="J" last="Mano">J. Mano</name><name sortKey="Sugiyama, K" sort="Sugiyama, K" uniqKey="Sugiyama K" first="K" last="Sugiyama">K. Sugiyama</name></noCountry><country name="Japon"><region name="Région du Kansai"><name sortKey="Izawa, S" sort="Izawa, S" uniqKey="Izawa S" first="S" last="Izawa">S. Izawa</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001086 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001086 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Bois
|area= GlutaredoxinV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:10497208
|texte= Thioredoxin deficiency causes the constitutive activation of Yap1, an AP-1-like transcription factor in Saccharomyces cerevisiae.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:10497208" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |