Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae.
Identifieur interne : 000D47 ( Main/Exploration ); précédent : 000D46; suivant : 000D48Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae.
Auteurs : Nuria Pujol-Carrion [Espagne] ; Gemma Belli ; Enrique Herrero ; Antoni Nogues ; Maria Angeles De La Torre-RuizSource :
- Journal of cell science [ 0021-9533 ] ; 2006.
Descripteurs français
- KwdFr :
- ARN fongique (génétique), ARN fongique (métabolisme), Activation de la transcription (physiologie), Cycle cellulaire (physiologie), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Fer (métabolisme), Glutarédoxines (MeSH), Immunoprécipitation (MeSH), Noyau de la cellule (métabolisme), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydants (pharmacologie), Oxydoréduction (MeSH), Peroxyde d'hydrogène (pharmacologie), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Stress oxydatif (MeSH), Technique de Northern (MeSH), Techniques de double hybride (MeSH), Transport des protéines (MeSH).
- MESH :
- génétique : ARN fongique, Facteurs de transcription, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : ARN fongique, Facteurs de transcription, Fer, Noyau de la cellule, Oxidoreductases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Oxydants, Peroxyde d'hydrogène.
- physiologie : Activation de la transcription, Cycle cellulaire.
- Glutarédoxines, Immunoprécipitation, Oxydoréduction, Régulation de l'expression des gènes fongiques, Stress oxydatif, Technique de Northern, Techniques de double hybride, Transport des protéines.
English descriptors
- KwdEn :
- Blotting, Northern (MeSH), Cell Cycle (physiology), Cell Nucleus (metabolism), Gene Expression Regulation, Fungal (MeSH), Glutaredoxins (MeSH), Hydrogen Peroxide (pharmacology), Immunoprecipitation (MeSH), Iron (metabolism), Oxidants (pharmacology), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Protein Transport (MeSH), RNA, Fungal (genetics), RNA, Fungal (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Transcription Factors (genetics), Transcription Factors (metabolism), Transcriptional Activation (physiology), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , genetics : Oxidoreductases, RNA, Fungal, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , metabolism : Iron, Oxidoreductases, RNA, Fungal, Saccharomyces cerevisiae Proteins, Transcription Factors.
- chemical , pharmacology : Hydrogen Peroxide, Oxidants.
- chemical : Glutaredoxins.
- genetics : Saccharomyces cerevisiae.
- metabolism : Cell Nucleus, Saccharomyces cerevisiae.
- physiology : Cell Cycle, Transcriptional Activation.
- Blotting, Northern, Gene Expression Regulation, Fungal, Immunoprecipitation, Oxidation-Reduction, Oxidative Stress, Protein Transport, Two-Hybrid System Techniques.
Abstract
Grx3 and Grx4, two monothiol glutaredoxins of Saccharomyces cerevisiae, regulate Aft1 nuclear localisation. We provide evidence of a negative regulation of Aft1 activity by Grx3 and Grx4. The Grx domain of both proteins played an important role in Aft1 translocation to the cytoplasm. This function was not, however, dependent on the availability of iron. Here we demonstrate that Grx3, Grx4 and Aft1 interact each other both in vivo and in vitro, which suggests the existence of a functional protein complex. Interestingly, each interaction occurred independently on the third member of the complex. The absence of both Grx3 and Grx4 induced a clear enrichment of G1 cells in asynchronous cultures, a slow growth phenotype, the accumulation of intracellular iron and a constitutive activation of the genes regulated by Aft1. The grx3grx4 double mutant was highly sensitive to the oxidising agents hydrogen peroxide and t-butylhydroperoxide but not to diamide. The phenotypes of the double mutant grx3grx4 characterised in this study were mainly mediated by the Aft1 function, suggesting that grx3grx4 could be a suitable cellular model for studying endogenous oxidative stress induced by deregulation of the iron homeostasis. However, our results also suggest that Grx3 and Grx4 might play additional roles in the oxidative stress response through proteins other than Aft1.
DOI: 10.1242/jcs.03229
PubMed: 17074835
Affiliations:
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(pharmacology)</term><term>Immunoprecipitation (MeSH)</term><term>Iron (metabolism)</term><term>Oxidants (pharmacology)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Protein Transport (MeSH)</term><term>RNA, Fungal (genetics)</term><term>RNA, Fungal (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>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term><term>Transcriptional Activation (physiology)</term><term>Two-Hybrid System Techniques (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN fongique (génétique)</term><term>ARN fongique (métabolisme)</term><term>Activation de la transcription (physiologie)</term><term>Cycle 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qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term><term>RNA, Fungal</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Iron</term><term>Oxidoreductases</term><term>RNA, Fungal</term><term>Saccharomyces cerevisiae Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</term><term>Oxidants</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN fongique</term><term>Facteurs de transcription</term><term>Oxidoreductases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces 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Fungal</term><term>Immunoprecipitation</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Protein Transport</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Glutarédoxines</term><term>Immunoprécipitation</term><term>Oxydoréduction</term><term>Régulation de l'expression des gènes fongiques</term><term>Stress oxydatif</term><term>Technique de Northern</term><term>Techniques de double hybride</term><term>Transport des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Grx3 and Grx4, two monothiol glutaredoxins of Saccharomyces cerevisiae, regulate Aft1 nuclear localisation. We provide evidence of a negative regulation of Aft1 activity by Grx3 and Grx4. The Grx domain of both proteins played an important role in Aft1 translocation to the cytoplasm. This function was not, however, dependent on the availability of iron. Here we demonstrate that Grx3, Grx4 and Aft1 interact each other both in vivo and in vitro, which suggests the existence of a functional protein complex. Interestingly, each interaction occurred independently on the third member of the complex. The absence of both Grx3 and Grx4 induced a clear enrichment of G1 cells in asynchronous cultures, a slow growth phenotype, the accumulation of intracellular iron and a constitutive activation of the genes regulated by Aft1. The grx3grx4 double mutant was highly sensitive to the oxidising agents hydrogen peroxide and t-butylhydroperoxide but not to diamide. The phenotypes of the double mutant grx3grx4 characterised in this study were mainly mediated by the Aft1 function, suggesting that grx3grx4 could be a suitable cellular model for studying endogenous oxidative stress induced by deregulation of the iron homeostasis. However, our results also suggest that Grx3 and Grx4 might play additional roles in the oxidative stress response through proteins other than Aft1.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17074835</PMID><DateCompleted><Year>2007</Year><Month>01</Month><Day>16</Day></DateCompleted><DateRevised><Year>2014</Year><Month>11</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9533</ISSN><JournalIssue CitedMedium="Print"><Volume>119</Volume><Issue>Pt 21</Issue><PubDate><Year>2006</Year><Month>Nov</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J Cell Sci</ISOAbbreviation></Journal><ArticleTitle>Glutaredoxins Grx3 and Grx4 regulate nuclear localisation of Aft1 and the oxidative stress response in Saccharomyces cerevisiae.</ArticleTitle><Pagination><MedlinePgn>4554-64</MedlinePgn></Pagination><Abstract><AbstractText>Grx3 and Grx4, two monothiol glutaredoxins of Saccharomyces cerevisiae, regulate Aft1 nuclear localisation. We provide evidence of a negative regulation of Aft1 activity by Grx3 and Grx4. The Grx domain of both proteins played an important role in Aft1 translocation to the cytoplasm. This function was not, however, dependent on the availability of iron. Here we demonstrate that Grx3, Grx4 and Aft1 interact each other both in vivo and in vitro, which suggests the existence of a functional protein complex. Interestingly, each interaction occurred independently on the third member of the complex. The absence of both Grx3 and Grx4 induced a clear enrichment of G1 cells in asynchronous cultures, a slow growth phenotype, the accumulation of intracellular iron and a constitutive activation of the genes regulated by Aft1. The grx3grx4 double mutant was highly sensitive to the oxidising agents hydrogen peroxide and t-butylhydroperoxide but not to diamide. The phenotypes of the double mutant grx3grx4 characterised in this study were mainly mediated by the Aft1 function, suggesting that grx3grx4 could be a suitable cellular model for studying endogenous oxidative stress induced by deregulation of the iron homeostasis. However, our results also suggest that Grx3 and Grx4 might play additional roles in the oxidative stress response through proteins other than Aft1.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pujol-Carrion</LastName><ForeName>Nuria</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Universitat de Lleida, Lleida 25198, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Belli</LastName><ForeName>Gemma</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Nogues</LastName><ForeName>Antoni</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>de la Torre-Ruiz</LastName><ForeName>Maria Angeles</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C090297">AFT1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516012">Grx4 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016877">Oxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012331">RNA, Fungal</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>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>E1UOL152H7</RegistryNumber><NameOfSubstance UI="D007501">Iron</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015152" MajorTopicYN="N">Blotting, Northern</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002453" MajorTopicYN="N">Cell Cycle</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002467" MajorTopicYN="N">Cell Nucleus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D047468" MajorTopicYN="N">Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007501" MajorTopicYN="N">Iron</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016877" MajorTopicYN="N">Oxidants</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="Y">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012331" MajorTopicYN="N">RNA, Fungal</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><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="N">Saccharomyces cerevisiae Proteins</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="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015533" MajorTopicYN="N">Transcriptional Activation</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>11</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>1</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>11</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17074835</ArticleId><ArticleId IdType="pii">119/21/4554</ArticleId><ArticleId IdType="doi">10.1242/jcs.03229</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Catalogne</li></region></list><tree><noCountry><name sortKey="Belli, Gemma" sort="Belli, Gemma" uniqKey="Belli G" first="Gemma" last="Belli">Gemma Belli</name><name sortKey="De La Torre Ruiz, Maria Angeles" sort="De La Torre Ruiz, Maria Angeles" uniqKey="De La Torre Ruiz M" first="Maria Angeles" last="De La Torre-Ruiz">Maria Angeles De La Torre-Ruiz</name><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name><name sortKey="Nogues, Antoni" sort="Nogues, Antoni" uniqKey="Nogues A" first="Antoni" last="Nogues">Antoni Nogues</name></noCountry><country name="Espagne"><region name="Catalogne"><name sortKey="Pujol Carrion, Nuria" sort="Pujol Carrion, Nuria" uniqKey="Pujol Carrion N" first="Nuria" last="Pujol-Carrion">Nuria Pujol-Carrion</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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