Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress.
Identifieur interne : 001043 ( Main/Exploration ); précédent : 001042; suivant : 001044Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress.
Auteurs : M J Prieto-Alamo [Espagne] ; J. Jurado ; R. Gallardo-Madueno ; F. Monje-Casas ; A. Holmgren ; C. PueyoSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2000.
Descripteurs français
- KwdFr :
- Escherichia coli (MeSH), Glutarédoxines (MeSH), Oxidoreductases (MeSH), Protéines (génétique), Protéines (métabolisme), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Régulation de l'expression des gènes bactériens (MeSH), Stress oxydatif (MeSH), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Transcription génétique (MeSH).
- MESH :
English descriptors
- KwdEn :
- Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Escherichia coli (MeSH), Gene Expression Regulation, Bacterial (MeSH), Glutaredoxins (MeSH), Oxidative Stress (MeSH), Oxidoreductases (MeSH), Proteins (genetics), Proteins (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism), Transcription, Genetic (MeSH).
- MESH :
- chemical , genetics : Bacterial Proteins, Proteins, Thioredoxins.
- chemical , metabolism : Bacterial Proteins, Proteins, Thioredoxins.
- Escherichia coli, Gene Expression Regulation, Bacterial, Glutaredoxins, Oxidative Stress, Oxidoreductases, Transcription, Genetic.
Abstract
We examined the in vivo expression of up to 16 genes encoding for components of both glutaredoxin and thioredoxin systems and for members of the OxyR and SoxRS regulons. We demonstrated that grxA (Grx1) transcription is triggered in bacteria lacking Trx1 (trxA) and GSH (gshA) in an OxyR-dependent manner. We also indicated that, unlike OxyR, SoxR is not constitutively activated in the oxidizing environment of trxA gshA mutants. We discovered that the lack of Trx1 plus GSH increases the steady-state levels of Trx reductase (trxB) and Trx2 (trxC) transcripts. This increase and the trxB and trxC up-regulation caused by the constitutive oxyR2 allele indicate that OxyR also plays a role in the regulation of the thioredoxin pathway. On the contrary, no change in the expression of genes for Trx1, Grx2, and Grx3 was observed. Transcription of nrdAB (RRase) was not induced by oxidative stress yet was induced by hydroxyurea (RRase inhibitor). Induction level was as the enhanced nrdAB basal expression of trxA grxA mutants, indicating that RRase operation without Trx1 and Grx1 must lead to disturbances sensed as those caused by hydroxyurea. We also demonstrated an inverse relation between nrdAB expression and that of genes coding for components of both glutaredoxin (grxA, gorA) and thioredoxin (trxB, trxC) systems.
DOI: 10.1074/jbc.275.18.13398
PubMed: 10788450
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress.</title><author><name sortKey="Prieto Alamo, M J" sort="Prieto Alamo, M J" uniqKey="Prieto Alamo M" first="M J" last="Prieto-Alamo">M J Prieto-Alamo</name><affiliation wicri:level="2"><nlm:affiliation>Departamento de Bioquimica y Biologia Molecular, Universidad de Córdoba, 14071-Córdoba, España.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Bioquimica y Biologia Molecular, Universidad de Córdoba, 14071-Córdoba</wicri:regionArea><placeName><region nuts="2" type="communauté">Andalousie</region></placeName></affiliation></author><author><name sortKey="Jurado, J" sort="Jurado, J" uniqKey="Jurado J" first="J" last="Jurado">J. Jurado</name></author><author><name sortKey="Gallardo Madueno, R" sort="Gallardo Madueno, R" uniqKey="Gallardo Madueno R" first="R" last="Gallardo-Madueno">R. Gallardo-Madueno</name></author><author><name sortKey="Monje Casas, F" sort="Monje Casas, F" uniqKey="Monje Casas F" first="F" last="Monje-Casas">F. Monje-Casas</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2000">2000</date><idno type="RBID">pubmed:10788450</idno><idno type="pmid">10788450</idno><idno type="doi">10.1074/jbc.275.18.13398</idno><idno type="wicri:Area/Main/Corpus">001078</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001078</idno><idno type="wicri:Area/Main/Curation">001078</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001078</idno><idno type="wicri:Area/Main/Exploration">001078</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress.</title><author><name sortKey="Prieto Alamo, M J" sort="Prieto Alamo, M J" uniqKey="Prieto Alamo M" first="M J" last="Prieto-Alamo">M J Prieto-Alamo</name><affiliation wicri:level="2"><nlm:affiliation>Departamento de Bioquimica y Biologia Molecular, Universidad de Córdoba, 14071-Córdoba, España.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Bioquimica y Biologia Molecular, Universidad de Córdoba, 14071-Córdoba</wicri:regionArea><placeName><region nuts="2" type="communauté">Andalousie</region></placeName></affiliation></author><author><name sortKey="Jurado, J" sort="Jurado, J" uniqKey="Jurado J" first="J" last="Jurado">J. Jurado</name></author><author><name sortKey="Gallardo Madueno, R" sort="Gallardo Madueno, R" uniqKey="Gallardo Madueno R" first="R" last="Gallardo-Madueno">R. Gallardo-Madueno</name></author><author><name sortKey="Monje Casas, F" sort="Monje Casas, F" uniqKey="Monje Casas F" first="F" last="Monje-Casas">F. Monje-Casas</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</name></author></analytic><series><title level="j">The Journal of biological chemistry</title><idno type="ISSN">0021-9258</idno><imprint><date when="2000" type="published">2000</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (genetics)</term><term>Bacterial Proteins (metabolism)</term><term>Escherichia coli (MeSH)</term><term>Gene Expression Regulation, Bacterial (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (genetics)</term><term>Proteins (metabolism)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term><term>Transcription, Genetic (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Escherichia coli (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (génétique)</term><term>Protéines (métabolisme)</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Régulation de l'expression des gènes bactériens (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term><term>Transcription génétique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines</term><term>Protéines bactériennes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines</term><term>Protéines bactériennes</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Escherichia coli</term><term>Gene Expression Regulation, Bacterial</term><term>Glutaredoxins</term><term>Oxidative Stress</term><term>Oxidoreductases</term><term>Transcription, Genetic</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Escherichia coli</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Régulation de l'expression des gènes bactériens</term><term>Stress oxydatif</term><term>Transcription génétique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We examined the in vivo expression of up to 16 genes encoding for components of both glutaredoxin and thioredoxin systems and for members of the OxyR and SoxRS regulons. We demonstrated that grxA (Grx1) transcription is triggered in bacteria lacking Trx1 (trxA) and GSH (gshA) in an OxyR-dependent manner. We also indicated that, unlike OxyR, SoxR is not constitutively activated in the oxidizing environment of trxA gshA mutants. We discovered that the lack of Trx1 plus GSH increases the steady-state levels of Trx reductase (trxB) and Trx2 (trxC) transcripts. This increase and the trxB and trxC up-regulation caused by the constitutive oxyR2 allele indicate that OxyR also plays a role in the regulation of the thioredoxin pathway. On the contrary, no change in the expression of genes for Trx1, Grx2, and Grx3 was observed. Transcription of nrdAB (RRase) was not induced by oxidative stress yet was induced by hydroxyurea (RRase inhibitor). Induction level was as the enhanced nrdAB basal expression of trxA grxA mutants, indicating that RRase operation without Trx1 and Grx1 must lead to disturbances sensed as those caused by hydroxyurea. We also demonstrated an inverse relation between nrdAB expression and that of genes coding for components of both glutaredoxin (grxA, gorA) and thioredoxin (trxB, trxC) systems.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10788450</PMID><DateCompleted><Year>2000</Year><Month>06</Month><Day>01</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>275</Volume><Issue>18</Issue><PubDate><Year>2000</Year><Month>May</Month><Day>05</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress.</ArticleTitle><Pagination><MedlinePgn>13398-405</MedlinePgn></Pagination><Abstract><AbstractText>We examined the in vivo expression of up to 16 genes encoding for components of both glutaredoxin and thioredoxin systems and for members of the OxyR and SoxRS regulons. We demonstrated that grxA (Grx1) transcription is triggered in bacteria lacking Trx1 (trxA) and GSH (gshA) in an OxyR-dependent manner. We also indicated that, unlike OxyR, SoxR is not constitutively activated in the oxidizing environment of trxA gshA mutants. We discovered that the lack of Trx1 plus GSH increases the steady-state levels of Trx reductase (trxB) and Trx2 (trxC) transcripts. This increase and the trxB and trxC up-regulation caused by the constitutive oxyR2 allele indicate that OxyR also plays a role in the regulation of the thioredoxin pathway. On the contrary, no change in the expression of genes for Trx1, Grx2, and Grx3 was observed. Transcription of nrdAB (RRase) was not induced by oxidative stress yet was induced by hydroxyurea (RRase inhibitor). Induction level was as the enhanced nrdAB basal expression of trxA grxA mutants, indicating that RRase operation without Trx1 and Grx1 must lead to disturbances sensed as those caused by hydroxyurea. We also demonstrated an inverse relation between nrdAB expression and that of genes coding for components of both glutaredoxin (grxA, gorA) and thioredoxin (trxB, trxC) systems.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Prieto-Alamo</LastName><ForeName>M J</ForeName><Initials>MJ</Initials><AffiliationInfo><Affiliation>Departamento de Bioquimica y Biologia Molecular, Universidad de Córdoba, 14071-Córdoba, España.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jurado</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Gallardo-Madueno</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Monje-Casas</LastName><ForeName>F</ForeName><Initials>F</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Pueyo</LastName><ForeName>C</ForeName><Initials>C</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>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial 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>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="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015964" MajorTopicYN="Y">Gene Expression Regulation, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="Y">Transcription, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2000</Year><Month>5</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2000</Year><Month>6</Month><Day>3</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2000</Year><Month>5</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10788450</ArticleId><ArticleId IdType="pii">275/18/13398</ArticleId><ArticleId IdType="doi">10.1074/jbc.275.18.13398</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Andalousie</li></region></list><tree><noCountry><name sortKey="Gallardo Madueno, R" sort="Gallardo Madueno, R" uniqKey="Gallardo Madueno R" first="R" last="Gallardo-Madueno">R. Gallardo-Madueno</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Jurado, J" sort="Jurado, J" uniqKey="Jurado J" first="J" last="Jurado">J. Jurado</name><name sortKey="Monje Casas, F" sort="Monje Casas, F" uniqKey="Monje Casas F" first="F" last="Monje-Casas">F. Monje-Casas</name><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</name></noCountry><country name="Espagne"><region name="Andalousie"><name sortKey="Prieto Alamo, M J" sort="Prieto Alamo, M J" uniqKey="Prieto Alamo M" first="M J" last="Prieto-Alamo">M J Prieto-Alamo</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 001043 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 001043 | 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:10788450
|texte= Transcriptional regulation of glutaredoxin and thioredoxin pathways and related enzymes in response to oxidative stress.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:10788450" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a GlutaredoxinV1
| This area was generated with Dilib version V0.6.37. |  |