Mouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2.
Identifieur interne : 001100 ( Main/Exploration ); précédent : 001099; suivant : 001101Mouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2.
Auteurs : T. Nakamura [Japon] ; T. Ohno ; K. Hirota ; A. Nishiyama ; H. Nakamura ; H. Wada ; J. YodoiSource :
- Free radical research [ 1071-5762 ] ; 1999.
Descripteurs français
- KwdFr :
- ADN (génétique), ADN (métabolisme), ADN complémentaire (génétique), ADN complémentaire (isolement et purification), Animaux (MeSH), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (MeSH), Facteur de transcription AP-2 (MeSH), Facteurs de transcription (génétique), Facteurs de transcription (métabolisme), Glutarédoxines (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (génétique), Protéines (métabolisme), Protéines de liaison à l'ADN (génétique), Protéines de liaison à l'ADN (métabolisme), Souris (MeSH), Stress oxydatif (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- génétique : ADN, ADN complémentaire, Facteurs de transcription, Protéines, Protéines de liaison à l'ADN.
- isolement et purification : ADN complémentaire.
- métabolisme : ADN, Facteurs de transcription, Protéines, Protéines de liaison à l'ADN.
- Animaux, Clonage moléculaire, Données de séquences moléculaires, Escherichia coli, Facteur de transcription AP-2, Glutarédoxines, Oxidoreductases, Oxydoréduction, Souris, Stress oxydatif, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Base Sequence (MeSH), Cloning, Molecular (MeSH), DNA (genetics), DNA (metabolism), DNA, Complementary (genetics), DNA, Complementary (isolation & purification), DNA-Binding Proteins (genetics), DNA-Binding Proteins (metabolism), Escherichia coli (MeSH), Glutaredoxins (MeSH), Mice (MeSH), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (MeSH), Proteins (genetics), Proteins (metabolism), Transcription Factor AP-2 (MeSH), Transcription Factors (genetics), Transcription Factors (metabolism).
- MESH :
- chemical , genetics : DNA, DNA, Complementary, DNA-Binding Proteins, Proteins, Transcription Factors.
- chemical , isolation & purification : DNA, Complementary.
- chemical , metabolism : DNA, DNA-Binding Proteins, Proteins, Transcription Factors.
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Escherichia coli, Glutaredoxins, Mice, Molecular Sequence Data, Oxidation-Reduction, Oxidative Stress, Oxidoreductases, Transcription Factor AP-2.
Abstract
We have isolated a cDNA encoding glutaredoxin (GRX) from a mouse splenic cDNA library. This cDNA encoded a protein of 107 amino acids with a calculated molecular weight of 11.9 kDa. The deduced amino acid sequence of glutaredoxin in mouse was highly homologous with that in other mammals (81-89%), containing a putative active sequence of -Cys-Pro-Try-Cys-. Recombinant mouse glutaredoxin expressed in E. coli showed glutathione-disulfide oxidoreductase activity with beta-hydroxyethyl disulfide as its substrate, whereas mutant glutaredoxin (Cys 22, Cys 25 to Ser) showed no activity. In electrophoretic mobility shift assay, we proved that wild type GRX, not mutant one, recovered the DNA-binding activity of a transcription factor, PEBP2, oxidized by diamide. This showed that GRX may be involved in the redox regulation of the DNA-binding activity of PEBP2 as is the case with thioredoxin.
DOI: 10.1080/10715769900300931
PubMed: 10517541
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Ohno</name></author><author><name sortKey="Hirota, K" sort="Hirota, K" uniqKey="Hirota K" first="K" last="Hirota">K. Hirota</name></author><author><name sortKey="Nishiyama, A" sort="Nishiyama, A" uniqKey="Nishiyama A" first="A" last="Nishiyama">A. Nishiyama</name></author><author><name sortKey="Nakamura, H" sort="Nakamura, H" uniqKey="Nakamura H" first="H" last="Nakamura">H. Nakamura</name></author><author><name sortKey="Wada, H" sort="Wada, H" uniqKey="Wada H" first="H" last="Wada">H. Wada</name></author><author><name sortKey="Yodoi, J" sort="Yodoi, J" uniqKey="Yodoi J" first="J" last="Yodoi">J. Yodoi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10517541</idno><idno type="pmid">10517541</idno><idno type="doi">10.1080/10715769900300931</idno><idno type="wicri:Area/Main/Corpus">001093</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001093</idno><idno type="wicri:Area/Main/Curation">001093</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001093</idno><idno type="wicri:Area/Main/Exploration">001093</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Mouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2.</title><author><name sortKey="Nakamura, T" sort="Nakamura, T" uniqKey="Nakamura T" first="T" last="Nakamura">T. Nakamura</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biological Responses, Institute for Virus Research, Kyoto University, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Biological Responses, Institute for Virus Research, Kyoto University</wicri:regionArea><placeName><settlement type="city">Kyoto</settlement><region type="prefecture">Région du Kansai</region></placeName><orgName type="university">Université de Kyoto</orgName></affiliation></author><author><name sortKey="Ohno, T" sort="Ohno, T" uniqKey="Ohno T" first="T" last="Ohno">T. Ohno</name></author><author><name sortKey="Hirota, K" sort="Hirota, K" uniqKey="Hirota K" first="K" last="Hirota">K. Hirota</name></author><author><name sortKey="Nishiyama, A" sort="Nishiyama, A" uniqKey="Nishiyama A" first="A" last="Nishiyama">A. Nishiyama</name></author><author><name sortKey="Nakamura, H" sort="Nakamura, H" uniqKey="Nakamura H" first="H" last="Nakamura">H. Nakamura</name></author><author><name sortKey="Wada, H" sort="Wada, H" uniqKey="Wada H" first="H" last="Wada">H. Wada</name></author><author><name sortKey="Yodoi, J" sort="Yodoi, J" uniqKey="Yodoi J" first="J" last="Yodoi">J. Yodoi</name></author></analytic><series><title level="j">Free radical research</title><idno type="ISSN">1071-5762</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Base Sequence (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>DNA (genetics)</term><term>DNA (metabolism)</term><term>DNA, Complementary (genetics)</term><term>DNA, Complementary (isolation & purification)</term><term>DNA-Binding Proteins (genetics)</term><term>DNA-Binding Proteins (metabolism)</term><term>Escherichia coli (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Mice (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (genetics)</term><term>Proteins (metabolism)</term><term>Transcription Factor AP-2 (MeSH)</term><term>Transcription Factors (genetics)</term><term>Transcription Factors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN (génétique)</term><term>ADN (métabolisme)</term><term>ADN complémentaire (génétique)</term><term>ADN complémentaire (isolement et purification)</term><term>Animaux (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Escherichia coli (MeSH)</term><term>Facteur de transcription AP-2 (MeSH)</term><term>Facteurs de transcription (génétique)</term><term>Facteurs de transcription (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (génétique)</term><term>Protéines (métabolisme)</term><term>Protéines de liaison à l'ADN (génétique)</term><term>Protéines de liaison à l'ADN (métabolisme)</term><term>Souris (MeSH)</term><term>Stress oxydatif (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Séquence nucléotidique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA</term><term>DNA, Complementary</term><term>DNA-Binding Proteins</term><term>Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>DNA, Complementary</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>DNA</term><term>DNA-Binding Proteins</term><term>Proteins</term><term>Transcription Factors</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN</term><term>ADN complémentaire</term><term>Facteurs de transcription</term><term>Protéines</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>ADN complémentaire</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADN</term><term>Facteurs de transcription</term><term>Protéines</term><term>Protéines de liaison à l'ADN</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Base Sequence</term><term>Cloning, Molecular</term><term>Escherichia coli</term><term>Glutaredoxins</term><term>Mice</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Oxidoreductases</term><term>Transcription Factor AP-2</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Escherichia coli</term><term>Facteur de transcription AP-2</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Souris</term><term>Stress oxydatif</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We have isolated a cDNA encoding glutaredoxin (GRX) from a mouse splenic cDNA library. This cDNA encoded a protein of 107 amino acids with a calculated molecular weight of 11.9 kDa. The deduced amino acid sequence of glutaredoxin in mouse was highly homologous with that in other mammals (81-89%), containing a putative active sequence of -Cys-Pro-Try-Cys-. Recombinant mouse glutaredoxin expressed in E. coli showed glutathione-disulfide oxidoreductase activity with beta-hydroxyethyl disulfide as its substrate, whereas mutant glutaredoxin (Cys 22, Cys 25 to Ser) showed no activity. In electrophoretic mobility shift assay, we proved that wild type GRX, not mutant one, recovered the DNA-binding activity of a transcription factor, PEBP2, oxidized by diamide. This showed that GRX may be involved in the redox regulation of the DNA-binding activity of PEBP2 as is the case with thioredoxin.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10517541</PMID><DateCompleted><Year>1999</Year><Month>11</Month><Day>09</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1071-5762</ISSN><JournalIssue CitedMedium="Print"><Volume>31</Volume><Issue>4</Issue><PubDate><Year>1999</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Free radical research</Title><ISOAbbreviation>Free Radic Res</ISOAbbreviation></Journal><ArticleTitle>Mouse glutaredoxin - cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2.</ArticleTitle><Pagination><MedlinePgn>357-65</MedlinePgn></Pagination><Abstract><AbstractText>We have isolated a cDNA encoding glutaredoxin (GRX) from a mouse splenic cDNA library. This cDNA encoded a protein of 107 amino acids with a calculated molecular weight of 11.9 kDa. The deduced amino acid sequence of glutaredoxin in mouse was highly homologous with that in other mammals (81-89%), containing a putative active sequence of -Cys-Pro-Try-Cys-. Recombinant mouse glutaredoxin expressed in E. coli showed glutathione-disulfide oxidoreductase activity with beta-hydroxyethyl disulfide as its substrate, whereas mutant glutaredoxin (Cys 22, Cys 25 to Ser) showed no activity. In electrophoretic mobility shift assay, we proved that wild type GRX, not mutant one, recovered the DNA-binding activity of a transcription factor, PEBP2, oxidized by diamide. This showed that GRX may be involved in the redox regulation of the DNA-binding activity of PEBP2 as is the case with thioredoxin.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>T</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Department of Biological Responses, Institute for Virus Research, Kyoto University, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohno</LastName><ForeName>T</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Hirota</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Nishiyama</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Nakamura</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Wada</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Yodoi</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Free Radic Res</MedlineTA><NlmUniqueID>9423872</NlmUniqueID><ISSNLinking>1029-2470</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018076">DNA, Complementary</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="D050656">Transcription Factor AP-2</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014157">Transcription Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>9007-49-2</RegistryNumber><NameOfSubstance UI="D004247">DNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004247" MajorTopicYN="N">DNA</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018076" MajorTopicYN="N">DNA, Complementary</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004268" MajorTopicYN="N">DNA-Binding Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</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="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050656" MajorTopicYN="N">Transcription Factor AP-2</DescriptorName></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></MeshHeadingList><NumberOfReferences>43</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>10</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>10</Month><Day>12</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>10</Month><Day>12</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10517541</ArticleId><ArticleId IdType="doi">10.1080/10715769900300931</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="Hirota, K" sort="Hirota, K" uniqKey="Hirota K" first="K" last="Hirota">K. Hirota</name><name sortKey="Nakamura, H" sort="Nakamura, H" uniqKey="Nakamura H" first="H" last="Nakamura">H. Nakamura</name><name sortKey="Nishiyama, A" sort="Nishiyama, A" uniqKey="Nishiyama A" first="A" last="Nishiyama">A. Nishiyama</name><name sortKey="Ohno, T" sort="Ohno, T" uniqKey="Ohno T" first="T" last="Ohno">T. Ohno</name><name sortKey="Wada, H" sort="Wada, H" uniqKey="Wada H" first="H" last="Wada">H. Wada</name><name sortKey="Yodoi, J" sort="Yodoi, J" uniqKey="Yodoi J" first="J" last="Yodoi">J. Yodoi</name></noCountry><country name="Japon"><region name="Région du Kansai"><name sortKey="Nakamura, T" sort="Nakamura, T" uniqKey="Nakamura T" first="T" last="Nakamura">T. Nakamura</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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