Redox properties and evolution of human glutaredoxins.
Identifieur interne : 000C65 ( Main/Exploration ); précédent : 000C64; suivant : 000C66Redox properties and evolution of human glutaredoxins.
Auteurs : Johan Sagemark [Suède] ; Tobias H. Elgán ; Thomas R. Bürglin ; Catrine Johansson ; Arne Holmgren ; Kurt D. BerndtSource :
- Proteins [ 1097-0134 ] ; 2007.
Descripteurs français
- KwdFr :
- Cadres ouverts de lecture (MeSH), Cinétique (MeSH), Dichroïsme circulaire (MeSH), Disulfures (analyse), Disulfures (composition chimique), Dénaturation des protéines (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Plasmides (MeSH), Séquence conservée (MeSH), Séquence d'acides aminés (MeSH), Thermodynamique (MeSH), Évolution moléculaire (MeSH).
- MESH :
- analyse : Disulfures.
- composition chimique : Disulfures, Oxidoreductases.
- génétique : Oxidoreductases.
- métabolisme : Oxidoreductases.
- Cadres ouverts de lecture, Cinétique, Dichroïsme circulaire, Dénaturation des protéines, Glutarédoxines, Humains, Oxydoréduction, Plasmides, Séquence conservée, Séquence d'acides aminés, Thermodynamique, Évolution moléculaire.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Circular Dichroism (MeSH), Conserved Sequence (MeSH), Disulfides (analysis), Disulfides (chemistry), Evolution, Molecular (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Kinetics (MeSH), Open Reading Frames (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Plasmids (MeSH), Protein Denaturation (MeSH), Thermodynamics (MeSH).
- MESH :
- chemical , analysis : Disulfides.
- chemical , chemistry : Disulfides, Oxidoreductases.
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Oxidoreductases.
- Amino Acid Sequence, Circular Dichroism, Conserved Sequence, Evolution, Molecular, Glutaredoxins, Humans, Kinetics, Open Reading Frames, Oxidation-Reduction, Plasmids, Protein Denaturation, Thermodynamics.
Abstract
Glutaredoxins (Grxs) are glutathione-dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol-disulfide exchange reactions via active site cysteine residues. Focusing on the human dithiol glutaredoxins having a C-X-Y-C active site sequence motif, the redox potentials of hGrx1 and hGrx2 were determined to be -232 and -221 mV, respectively, using a combination of redox buffers, protein-protein equilibrium and thermodynamic linkage. In addition, a nonactive site disulfide was identified between Cys28 and Cys113 in hGrx2 using redox buffers and chemical digestion. This disulfide confers nearly five kcal mol(-1) additional stability by linking the C-terminal helix to the bulk of the protein. The redox potential of this nonactive site disulfide was determined to be -317 mV and is thus expected to be present in all but the most reducing conditions in vivo. As all human glutaredoxins contain additional nonactive site cysteine residues, a full phylogenetic analysis was performed to help elucidate their structural and functional roles. Three distinct groups were found: Grx1, Grx2, and Grx5, the latter representing a highly conserved group of monothiol glutaredoxins having a C-G-F-S active site sequence, with clear homologs from bacteria to human. Grx1 and Grx2 diverged from a common ancestor before the origin of vertebrates, possibly even earlier in animal evolution. The highly stabilizing nonactive site disulfide observed in hGrx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.
DOI: 10.1002/prot.21416
PubMed: 17546662
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Bürglin</name></author><author><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Berndt, Kurt D" sort="Berndt, Kurt D" uniqKey="Berndt K" first="Kurt D" last="Berndt">Kurt D. 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Elgán</name></author><author><name sortKey="Burglin, Thomas R" sort="Burglin, Thomas R" uniqKey="Burglin T" first="Thomas R" last="Bürglin">Thomas R. Bürglin</name></author><author><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author><author><name sortKey="Berndt, Kurt D" sort="Berndt, Kurt D" uniqKey="Berndt K" first="Kurt D" last="Berndt">Kurt D. Berndt</name></author></analytic><series><title level="j">Proteins</title><idno type="eISSN">1097-0134</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Circular Dichroism (MeSH)</term><term>Conserved Sequence (MeSH)</term><term>Disulfides (analysis)</term><term>Disulfides (chemistry)</term><term>Evolution, Molecular (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Open Reading Frames (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (chemistry)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Plasmids (MeSH)</term><term>Protein Denaturation (MeSH)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cadres ouverts de lecture (MeSH)</term><term>Cinétique (MeSH)</term><term>Dichroïsme circulaire (MeSH)</term><term>Disulfures (analyse)</term><term>Disulfures (composition chimique)</term><term>Dénaturation des protéines (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Plasmides (MeSH)</term><term>Séquence conservée (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Thermodynamique (MeSH)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Disulfides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Disulfures</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Conserved Sequence</term><term>Evolution, Molecular</term><term>Glutaredoxins</term><term>Humans</term><term>Kinetics</term><term>Open Reading Frames</term><term>Oxidation-Reduction</term><term>Plasmids</term><term>Protein Denaturation</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cadres ouverts de lecture</term><term>Cinétique</term><term>Dichroïsme circulaire</term><term>Dénaturation des protéines</term><term>Glutarédoxines</term><term>Humains</term><term>Oxydoréduction</term><term>Plasmides</term><term>Séquence conservée</term><term>Séquence d'acides aminés</term><term>Thermodynamique</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are glutathione-dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol-disulfide exchange reactions via active site cysteine residues. Focusing on the human dithiol glutaredoxins having a C-X-Y-C active site sequence motif, the redox potentials of hGrx1 and hGrx2 were determined to be -232 and -221 mV, respectively, using a combination of redox buffers, protein-protein equilibrium and thermodynamic linkage. In addition, a nonactive site disulfide was identified between Cys28 and Cys113 in hGrx2 using redox buffers and chemical digestion. This disulfide confers nearly five kcal mol(-1) additional stability by linking the C-terminal helix to the bulk of the protein. The redox potential of this nonactive site disulfide was determined to be -317 mV and is thus expected to be present in all but the most reducing conditions in vivo. As all human glutaredoxins contain additional nonactive site cysteine residues, a full phylogenetic analysis was performed to help elucidate their structural and functional roles. Three distinct groups were found: Grx1, Grx2, and Grx5, the latter representing a highly conserved group of monothiol glutaredoxins having a C-G-F-S active site sequence, with clear homologs from bacteria to human. Grx1 and Grx2 diverged from a common ancestor before the origin of vertebrates, possibly even earlier in animal evolution. The highly stabilizing nonactive site disulfide observed in hGrx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17546662</PMID><DateCompleted><Year>2007</Year><Month>10</Month><Day>01</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1097-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>68</Volume><Issue>4</Issue><PubDate><Year>2007</Year><Month>Sep</Month><Day>01</Day></PubDate></JournalIssue><Title>Proteins</Title><ISOAbbreviation>Proteins</ISOAbbreviation></Journal><ArticleTitle>Redox properties and evolution of human glutaredoxins.</ArticleTitle><Pagination><MedlinePgn>879-92</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (Grxs) are glutathione-dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol-disulfide exchange reactions via active site cysteine residues. Focusing on the human dithiol glutaredoxins having a C-X-Y-C active site sequence motif, the redox potentials of hGrx1 and hGrx2 were determined to be -232 and -221 mV, respectively, using a combination of redox buffers, protein-protein equilibrium and thermodynamic linkage. In addition, a nonactive site disulfide was identified between Cys28 and Cys113 in hGrx2 using redox buffers and chemical digestion. This disulfide confers nearly five kcal mol(-1) additional stability by linking the C-terminal helix to the bulk of the protein. The redox potential of this nonactive site disulfide was determined to be -317 mV and is thus expected to be present in all but the most reducing conditions in vivo. As all human glutaredoxins contain additional nonactive site cysteine residues, a full phylogenetic analysis was performed to help elucidate their structural and functional roles. Three distinct groups were found: Grx1, Grx2, and Grx5, the latter representing a highly conserved group of monothiol glutaredoxins having a C-G-F-S active site sequence, with clear homologs from bacteria to human. Grx1 and Grx2 diverged from a common ancestor before the origin of vertebrates, possibly even earlier in animal evolution. The highly stabilizing nonactive site disulfide observed in hGrx2 is found to be a conserved feature within the deuterostomes and appears to be the only additional conserved intramolecular disulfide within the glutaredoxins.</AbstractText><CopyrightInformation>2007 Wiley-Liss, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sagemark</LastName><ForeName>Johan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>School of Life Sciences, Södertörns Högskola, S-141 89 Huddinge, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Elgán</LastName><ForeName>Tobias H</ForeName><Initials>TH</Initials></Author><Author ValidYN="Y"><LastName>Bürglin</LastName><ForeName>Thomas R</ForeName><Initials>TR</Initials></Author><Author ValidYN="Y"><LastName>Johansson</LastName><ForeName>Catrine</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Berndt</LastName><ForeName>Kurt D</ForeName><Initials>KD</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>Proteins</MedlineTA><NlmUniqueID>8700181</NlmUniqueID><ISSNLinking>0887-3585</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</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="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>6</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>10</Month><Day>2</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>6</Month><Day>5</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17546662</ArticleId><ArticleId IdType="doi">10.1002/prot.21416</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Berndt, Kurt D" sort="Berndt, Kurt D" uniqKey="Berndt K" first="Kurt D" last="Berndt">Kurt D. Berndt</name><name sortKey="Burglin, Thomas R" sort="Burglin, Thomas R" uniqKey="Burglin T" first="Thomas R" last="Bürglin">Thomas R. Bürglin</name><name sortKey="Elgan, Tobias H" sort="Elgan, Tobias H" uniqKey="Elgan T" first="Tobias H" last="Elgán">Tobias H. Elgán</name><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name><name sortKey="Johansson, Catrine" sort="Johansson, Catrine" uniqKey="Johansson C" first="Catrine" last="Johansson">Catrine Johansson</name></noCountry><country name="Suède"><noRegion><name sortKey="Sagemark, Johan" sort="Sagemark, Johan" uniqKey="Sagemark J" first="Johan" last="Sagemark">Johan Sagemark</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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