Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin.
Identifieur interne : 000F49 ( Main/Exploration ); précédent : 000F48; suivant : 000F50Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin.
Auteurs : Jordi Tamarit [Espagne] ; Gemma Belli ; Elisa Cabiscol ; Enrique Herrero ; Joaquim RosSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2003.
Descripteurs français
- KwdFr :
- 2-Iodo-acétamide (pharmacologie), Antienzymes (pharmacologie), Biosynthèse des protéines (MeSH), Carbonic anhydrases (métabolisme), Catalyse (MeSH), Chromatographie en phase liquide à haute performance (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Cystéine (composition chimique), Cystéine (métabolisme), Disulfure de glutathion (métabolisme), Disulfures (métabolisme), Escherichia coli (métabolisme), Facteurs temps (MeSH), Glutarédoxines (MeSH), Glutathion (métabolisme), Mitochondries (métabolisme), Modèles biologiques (MeSH), Mutation (MeSH), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Oxygène (métabolisme), Plasmides (métabolisme), Protéines (composition chimique), Saccharomyces cerevisiae (métabolisme), Électrophysiologie (MeSH).
- MESH :
- composition chimique : Cystéine, Protéines.
- métabolisme : Carbonic anhydrases, Cystéine, Disulfure de glutathion, Disulfures, Escherichia coli, Glutathion, Mitochondries, Oxygène, Plasmides, Saccharomyces cerevisiae.
- pharmacologie : 2-Iodo-acétamide, Antienzymes.
- Biosynthèse des protéines, Catalyse, Chromatographie en phase liquide à haute performance, Cinétique, Concentration en ions d'hydrogène, Facteurs temps, Glutarédoxines, Modèles biologiques, Mutation, Oxidoreductases, Oxydoréduction, Électrophysiologie.
English descriptors
- KwdEn :
- Carbonic Anhydrases (metabolism), Catalysis (MeSH), Chromatography, High Pressure Liquid (MeSH), Cysteine (chemistry), Cysteine (metabolism), Disulfides (metabolism), Electrophysiology (MeSH), Enzyme Inhibitors (pharmacology), Escherichia coli (metabolism), Glutaredoxins (MeSH), Glutathione (metabolism), Glutathione Disulfide (metabolism), Hydrogen-Ion Concentration (MeSH), Iodoacetamide (pharmacology), Kinetics (MeSH), Mitochondria (metabolism), Models, Biological (MeSH), Mutation (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Oxygen (metabolism), Plasmids (metabolism), Protein Biosynthesis (MeSH), Proteins (chemistry), Saccharomyces cerevisiae (metabolism), Time Factors (MeSH).
- MESH :
- chemical , chemistry : Cysteine, Proteins.
- chemical , metabolism : Carbonic Anhydrases, Cysteine, Disulfides, Glutathione, Glutathione Disulfide, Oxygen.
- chemical , pharmacology : Enzyme Inhibitors, Iodoacetamide.
- metabolism : Escherichia coli, Mitochondria, Plasmids, Saccharomyces cerevisiae.
- Catalysis, Chromatography, High Pressure Liquid, Electrophysiology, Glutaredoxins, Hydrogen-Ion Concentration, Kinetics, Models, Biological, Mutation, Oxidation-Reduction, Oxidoreductases, Protein Biosynthesis, Time Factors.
Abstract
Grx5 is a yeast mitochondrial protein involved in iron-sulfur biogenesis that belongs to a recently described family of monothiolic glutaredoxin-like proteins. No member of this family has been biochemically characterized previously. Grx5 contains a conserved cysteine residue (Cys-60) and a non-conserved one (Cys-117). In this work, we have purified wild type and mutant C60S and C117S proteins and characterized their biochemical properties. A redox potential of -175 mV was calculated for wild type Grx5. The pKa values obtained by titration of mutant proteins with iodoacetamide at different pHs were 5.0 for Cys-60 and 8.2 for Cys-117. When Grx5 was incubated with glutathione disulfide, a transient mixed disulfide was formed between glutathione and the cystein 60 of the protein because of its low pKa. Binding of glutathione to Cys-60 promoted a decrease in the Cys-117 pKa value that triggered the formation of a disulfide bond between both cysteine residues of the protein, indicating that Cys-117 plays an essential role in the catalytic mechanism of Grx5. The disulfide bond in Grx5 could be reduced by GSH but at a rate at least 20 times slower than that observed for the reduction of glutaredoxin 1 from E. coli, a dithiolic glutaredoxin. This slow reduction rate could suggest that GSH may not be the physiologic reducing agent of Grx5. The fact that wild type Grx5 efficiently reduced a glutathiolated protein used as a substrate indicated that Grx5 may act as a thiol reductase inside the mitochondria.
DOI: 10.1074/jbc.M303477200
PubMed: 12730244
Affiliations:
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mitochondrial Grx5 monothiol glutaredoxin.</title><author><name sortKey="Tamarit, Jordi" sort="Tamarit, Jordi" uniqKey="Tamarit J" first="Jordi" last="Tamarit">Jordi Tamarit</name><affiliation wicri:level="2"><nlm:affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Rovira Roure 44, 25198 Lleida, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Rovira Roure 44, 25198 Lleida</wicri:regionArea><placeName><region nuts="2" type="communauté">Catalogne</region></placeName></affiliation></author><author><name sortKey="Belli, Gemma" sort="Belli, Gemma" uniqKey="Belli G" first="Gemma" last="Belli">Gemma Belli</name></author><author><name sortKey="Cabiscol, Elisa" sort="Cabiscol, Elisa" uniqKey="Cabiscol E" first="Elisa" last="Cabiscol">Elisa Cabiscol</name></author><author><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" 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Concentration (MeSH)</term><term>Iodoacetamide (pharmacology)</term><term>Kinetics (MeSH)</term><term>Mitochondria (metabolism)</term><term>Models, Biological (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxygen (metabolism)</term><term>Plasmids (metabolism)</term><term>Protein Biosynthesis (MeSH)</term><term>Proteins (chemistry)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Time Factors (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>2-Iodo-acétamide (pharmacologie)</term><term>Antienzymes (pharmacologie)</term><term>Biosynthèse des protéines (MeSH)</term><term>Carbonic anhydrases (métabolisme)</term><term>Catalyse (MeSH)</term><term>Chromatographie en phase liquide à haute performance (MeSH)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Cystéine (composition chimique)</term><term>Cystéine (métabolisme)</term><term>Disulfure de glutathion (métabolisme)</term><term>Disulfures (métabolisme)</term><term>Escherichia coli (métabolisme)</term><term>Facteurs temps (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>Mitochondries (métabolisme)</term><term>Modèles biologiques (MeSH)</term><term>Mutation (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Oxygène (métabolisme)</term><term>Plasmides (métabolisme)</term><term>Protéines (composition chimique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Électrophysiologie (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine</term><term>Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carbonic Anhydrases</term><term>Cysteine</term><term>Disulfides</term><term>Glutathione</term><term>Glutathione Disulfide</term><term>Oxygen</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Iodoacetamide</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cystéine</term><term>Protéines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Escherichia coli</term><term>Mitochondria</term><term>Plasmids</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Carbonic anhydrases</term><term>Cystéine</term><term>Disulfure de glutathion</term><term>Disulfures</term><term>Escherichia coli</term><term>Glutathion</term><term>Mitochondries</term><term>Oxygène</term><term>Plasmides</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>2-Iodo-acétamide</term><term>Antienzymes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalysis</term><term>Chromatography, High Pressure Liquid</term><term>Electrophysiology</term><term>Glutaredoxins</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Models, Biological</term><term>Mutation</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Protein Biosynthesis</term><term>Time Factors</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biosynthèse des protéines</term><term>Catalyse</term><term>Chromatographie en phase liquide à haute performance</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Facteurs temps</term><term>Glutarédoxines</term><term>Modèles biologiques</term><term>Mutation</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Électrophysiologie</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Grx5 is a yeast mitochondrial protein involved in iron-sulfur biogenesis that belongs to a recently described family of monothiolic glutaredoxin-like proteins. No member of this family has been biochemically characterized previously. Grx5 contains a conserved cysteine residue (Cys-60) and a non-conserved one (Cys-117). In this work, we have purified wild type and mutant C60S and C117S proteins and characterized their biochemical properties. A redox potential of -175 mV was calculated for wild type Grx5. The pKa values obtained by titration of mutant proteins with iodoacetamide at different pHs were 5.0 for Cys-60 and 8.2 for Cys-117. When Grx5 was incubated with glutathione disulfide, a transient mixed disulfide was formed between glutathione and the cystein 60 of the protein because of its low pKa. Binding of glutathione to Cys-60 promoted a decrease in the Cys-117 pKa value that triggered the formation of a disulfide bond between both cysteine residues of the protein, indicating that Cys-117 plays an essential role in the catalytic mechanism of Grx5. The disulfide bond in Grx5 could be reduced by GSH but at a rate at least 20 times slower than that observed for the reduction of glutaredoxin 1 from E. coli, a dithiolic glutaredoxin. This slow reduction rate could suggest that GSH may not be the physiologic reducing agent of Grx5. The fact that wild type Grx5 efficiently reduced a glutathiolated protein used as a substrate indicated that Grx5 may act as a thiol reductase inside the mitochondria.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12730244</PMID><DateCompleted><Year>2003</Year><Month>08</Month><Day>14</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>28</Issue><PubDate><Year>2003</Year><Month>Jul</Month><Day>11</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>25745-51</MedlinePgn></Pagination><Abstract><AbstractText>Grx5 is a yeast mitochondrial protein involved in iron-sulfur biogenesis that belongs to a recently described family of monothiolic glutaredoxin-like proteins. No member of this family has been biochemically characterized previously. Grx5 contains a conserved cysteine residue (Cys-60) and a non-conserved one (Cys-117). In this work, we have purified wild type and mutant C60S and C117S proteins and characterized their biochemical properties. A redox potential of -175 mV was calculated for wild type Grx5. The pKa values obtained by titration of mutant proteins with iodoacetamide at different pHs were 5.0 for Cys-60 and 8.2 for Cys-117. When Grx5 was incubated with glutathione disulfide, a transient mixed disulfide was formed between glutathione and the cystein 60 of the protein because of its low pKa. Binding of glutathione to Cys-60 promoted a decrease in the Cys-117 pKa value that triggered the formation of a disulfide bond between both cysteine residues of the protein, indicating that Cys-117 plays an essential role in the catalytic mechanism of Grx5. The disulfide bond in Grx5 could be reduced by GSH but at a rate at least 20 times slower than that observed for the reduction of glutaredoxin 1 from E. coli, a dithiolic glutaredoxin. This slow reduction rate could suggest that GSH may not be the physiologic reducing agent of Grx5. The fact that wild type Grx5 efficiently reduced a glutathiolated protein used as a substrate indicated that Grx5 may act as a thiol reductase inside the mitochondria.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tamarit</LastName><ForeName>Jordi</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Departament de Ciències Mèdiques Bàsiques, Facultat de Medicina, Universitat de Lleida, Rovira Roure 44, 25198 Lleida, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Belli</LastName><ForeName>Gemma</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Cabiscol</LastName><ForeName>Elisa</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Herrero</LastName><ForeName>Enrique</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Ros</LastName><ForeName>Joaquim</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2003</Year><Month>05</Month><Day>04</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="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 4.2.1.1</RegistryNumber><NameOfSubstance UI="D002256">Carbonic Anhydrases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>K848JZ4886</RegistryNumber><NameOfSubstance UI="D003545">Cysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical><Chemical><RegistryNumber>ULW86O013H</RegistryNumber><NameOfSubstance UI="D019803">Glutathione Disulfide</NameOfSubstance></Chemical><Chemical><RegistryNumber>ZRH8M27S79</RegistryNumber><NameOfSubstance UI="D007460">Iodoacetamide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002256" MajorTopicYN="N">Carbonic Anhydrases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004594" MajorTopicYN="N">Electrophysiology</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019803" MajorTopicYN="N">Glutathione Disulfide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007460" MajorTopicYN="N">Iodoacetamide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008954" MajorTopicYN="N">Models, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014176" MajorTopicYN="N">Protein Biosynthesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013997" MajorTopicYN="N">Time Factors</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>5</Month><Day>6</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>8</Month><Day>15</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>5</Month><Day>6</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12730244</ArticleId><ArticleId IdType="doi">10.1074/jbc.M303477200</ArticleId><ArticleId IdType="pii">M303477200</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="Cabiscol, Elisa" sort="Cabiscol, Elisa" uniqKey="Cabiscol E" first="Elisa" last="Cabiscol">Elisa Cabiscol</name><name sortKey="Herrero, Enrique" sort="Herrero, Enrique" uniqKey="Herrero E" first="Enrique" last="Herrero">Enrique Herrero</name><name sortKey="Ros, Joaquim" sort="Ros, Joaquim" uniqKey="Ros J" first="Joaquim" last="Ros">Joaquim Ros</name></noCountry><country name="Espagne"><region name="Catalogne"><name sortKey="Tamarit, Jordi" sort="Tamarit, Jordi" uniqKey="Tamarit J" first="Jordi" last="Tamarit">Jordi Tamarit</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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