Role of yeast glutaredoxins as glutathione S-transferases.
Identifieur interne : 000F10 ( Main/Exploration ); précédent : 000F09; suivant : 000F11Role of yeast glutaredoxins as glutathione S-transferases.
Auteurs : Emma J. Collinson [Royaume-Uni] ; Chris M. GrantSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2003.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Amorces ADN (MeSH), Cinétique (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Glutathione transferase (composition chimique), Glutathione transferase (génétique), Glutathione transferase (métabolisme), Génotype (MeSH), Mutagenèse dirigée (MeSH), Oxidoreductases (MeSH), Peroxyde d'hydrogène (pharmacologie), Plasmides (MeSH), Protéines (composition chimique), Protéines (génétique), Protéines (métabolisme), Protéines de Saccharomyces cerevisiae (composition chimique), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines recombinantes (métabolisme), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Glutathione transferase, Protéines, Protéines de Saccharomyces cerevisiae.
- enzymologie : Saccharomyces cerevisiae.
- génétique : Glutathione transferase, Protéines, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : Glutathione transferase, Protéines, Protéines de Saccharomyces cerevisiae, Protéines recombinantes, Saccharomyces cerevisiae.
- pharmacologie : Peroxyde d'hydrogène.
- Alignement de séquences, Amorces ADN, Cinétique, Données de séquences moléculaires, Glutarédoxines, Génotype, Mutagenèse dirigée, Oxidoreductases, Plasmides, Similitude de séquences d'acides aminés, Sites de fixation, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Binding Sites (MeSH), DNA Primers (MeSH), Genotype (MeSH), Glutaredoxins (MeSH), Glutathione Transferase (chemistry), Glutathione Transferase (genetics), Glutathione Transferase (metabolism), Hydrogen Peroxide (pharmacology), Kinetics (MeSH), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidoreductases (MeSH), Plasmids (MeSH), Proteins (chemistry), Proteins (genetics), Proteins (metabolism), Recombinant Proteins (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (chemistry), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Glutathione Transferase, Proteins, Saccharomyces cerevisiae Proteins.
- chemical , genetics : Glutathione Transferase, Proteins, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Glutathione Transferase, Proteins, Recombinant Proteins, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Hydrogen Peroxide.
- chemical : DNA Primers, Glutaredoxins, Oxidoreductases.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
- metabolism : Saccharomyces cerevisiae.
- Amino Acid Sequence, Base Sequence, Binding Sites, Genotype, Kinetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Plasmids, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
The yeast Saccharomyces cerevisiae contains two glutaredoxins, encoded by GRX1 and GRX2, that are required for resistance to reactive oxygen species. We recently reported that Grx1 is active as a glutathione peroxidase and can directly reduce hydroperoxides (Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., and Grant, C. M. (2002) J. Biol. Chem. 277, 16712-16717). We now show that Grx2 is also a general hydroperoxidase, and kinetic data indicate that both enzymes have a similar pattern of activity, which is highest with hydrogen peroxide, followed by cumene hydroperoxide and tert-butyl hydroperoxide. Furthermore, both Grx1 and Grx2 are shown be active as glutathione S-transferases (GSTs), and their activity with model substrates such as 1-chloro-2,4-dinitrobenzene is similar to their activity with hydroperoxides. Analysis of the Grx1 active site residues shows that Cys-27, but not Cys-30, is required for both the peroxidase and transferase activities, indicating that these reactions proceed via a monothiol mechanism. Deletion analysis shows that Grx1 and Grx2 have an overlapping function with yeast GSTs, encoded by GTT1 and GTT2, and are responsible for the majority of cellular GST activity. In addition, multiple mutants lacking GRX1, GRX2, GTT1, and GTT2 show increased sensitivity to stress conditions, including exposure to xenobiotics, heat, and oxidants. In summary, glutaredoxins are multifunctional enzymes with oxidoreductase, peroxidase, and GST activity, and are therefore ideally suited to detoxify the wide range of xenobiotics and oxidants that can be generated during diverse stress conditions.
DOI: 10.1074/jbc.M301387200
PubMed: 12684511
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Collinson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, Manchester M60 1QD, United Kingdom.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, Manchester M60 1QD</wicri:regionArea><wicri:noRegion>Manchester M60 1QD</wicri:noRegion></affiliation></author><author><name sortKey="Grant, Chris M" sort="Grant, Chris M" uniqKey="Grant C" first="Chris M" last="Grant">Chris M. 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xml:lang="en"><term>Glutathione Transferase</term><term>Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione Transferase</term><term>Proteins</term><term>Recombinant Proteins</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Hydrogen Peroxide</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>DNA Primers</term><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutathione transferase</term><term>Protéines</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces 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Sites</term><term>Genotype</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Plasmids</term><term>Sequence Alignment</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Amorces ADN</term><term>Cinétique</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Génotype</term><term>Mutagenèse dirigée</term><term>Oxidoreductases</term><term>Plasmides</term><term>Similitude de séquences d'acides aminés</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The yeast Saccharomyces cerevisiae contains two glutaredoxins, encoded by GRX1 and GRX2, that are required for resistance to reactive oxygen species. We recently reported that Grx1 is active as a glutathione peroxidase and can directly reduce hydroperoxides (Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., and Grant, C. M. (2002) J. Biol. Chem. 277, 16712-16717). We now show that Grx2 is also a general hydroperoxidase, and kinetic data indicate that both enzymes have a similar pattern of activity, which is highest with hydrogen peroxide, followed by cumene hydroperoxide and tert-butyl hydroperoxide. Furthermore, both Grx1 and Grx2 are shown be active as glutathione S-transferases (GSTs), and their activity with model substrates such as 1-chloro-2,4-dinitrobenzene is similar to their activity with hydroperoxides. Analysis of the Grx1 active site residues shows that Cys-27, but not Cys-30, is required for both the peroxidase and transferase activities, indicating that these reactions proceed via a monothiol mechanism. Deletion analysis shows that Grx1 and Grx2 have an overlapping function with yeast GSTs, encoded by GTT1 and GTT2, and are responsible for the majority of cellular GST activity. In addition, multiple mutants lacking GRX1, GRX2, GTT1, and GTT2 show increased sensitivity to stress conditions, including exposure to xenobiotics, heat, and oxidants. In summary, glutaredoxins are multifunctional enzymes with oxidoreductase, peroxidase, and GST activity, and are therefore ideally suited to detoxify the wide range of xenobiotics and oxidants that can be generated during diverse stress conditions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12684511</PMID><DateCompleted><Year>2003</Year><Month>08</Month><Day>21</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>278</Volume><Issue>25</Issue><PubDate><Year>2003</Year><Month>Jun</Month><Day>20</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Role of yeast glutaredoxins as glutathione S-transferases.</ArticleTitle><Pagination><MedlinePgn>22492-7</MedlinePgn></Pagination><Abstract><AbstractText>The yeast Saccharomyces cerevisiae contains two glutaredoxins, encoded by GRX1 and GRX2, that are required for resistance to reactive oxygen species. We recently reported that Grx1 is active as a glutathione peroxidase and can directly reduce hydroperoxides (Collinson, E. J., Wheeler, G. L., Garrido, E. O., Avery, A. M., Avery, S. V., and Grant, C. M. (2002) J. Biol. Chem. 277, 16712-16717). We now show that Grx2 is also a general hydroperoxidase, and kinetic data indicate that both enzymes have a similar pattern of activity, which is highest with hydrogen peroxide, followed by cumene hydroperoxide and tert-butyl hydroperoxide. Furthermore, both Grx1 and Grx2 are shown be active as glutathione S-transferases (GSTs), and their activity with model substrates such as 1-chloro-2,4-dinitrobenzene is similar to their activity with hydroperoxides. Analysis of the Grx1 active site residues shows that Cys-27, but not Cys-30, is required for both the peroxidase and transferase activities, indicating that these reactions proceed via a monothiol mechanism. Deletion analysis shows that Grx1 and Grx2 have an overlapping function with yeast GSTs, encoded by GTT1 and GTT2, and are responsible for the majority of cellular GST activity. In addition, multiple mutants lacking GRX1, GRX2, GTT1, and GTT2 show increased sensitivity to stress conditions, including exposure to xenobiotics, heat, and oxidants. In summary, glutaredoxins are multifunctional enzymes with oxidoreductase, peroxidase, and GST activity, and are therefore ideally suited to detoxify the wide range of xenobiotics and oxidants that can be generated during diverse stress conditions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Collinson</LastName><ForeName>Emma J</ForeName><Initials>EJ</Initials><AffiliationInfo><Affiliation>Department of Biomolecular Sciences, University of Manchester Institute of Science and Technology, Manchester M60 1QD, United Kingdom.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Grant</LastName><ForeName>Chris M</ForeName><Initials>CM</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><ArticleDate DateType="Electronic"><Year>2003</Year><Month>04</Month><Day>08</Day></ArticleDate></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="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>BBX060AN9V</RegistryNumber><NameOfSubstance UI="D006861">Hydrogen Peroxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.18</RegistryNumber><NameOfSubstance UI="D005982">Glutathione Transferase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001483" MajorTopicYN="N">Base Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017931" MajorTopicYN="N">DNA Primers</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005838" MajorTopicYN="N">Genotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005982" MajorTopicYN="N">Glutathione Transferase</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006861" MajorTopicYN="N">Hydrogen Peroxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016415" MajorTopicYN="N">Sequence Alignment</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>4</Month><Day>10</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>8</Month><Day>22</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>4</Month><Day>10</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12684511</ArticleId><ArticleId IdType="doi">10.1074/jbc.M301387200</ArticleId><ArticleId IdType="pii">M301387200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="Grant, Chris M" sort="Grant, Chris M" uniqKey="Grant C" first="Chris M" last="Grant">Chris M. Grant</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Collinson, Emma J" sort="Collinson, Emma J" uniqKey="Collinson E" first="Emma J" last="Collinson">Emma J. Collinson</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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