Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins.
Identifieur interne : 000B59 ( Main/Exploration ); précédent : 000B58; suivant : 000B60Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins.
Auteurs : Nikola Mesecke [Allemagne] ; Sarah Mittler ; Elisabeth Eckers ; Johannes M. Herrmann ; Marcel DeponteSource :
- Biochemistry [ 0006-2960 ] ; 2008.
Descripteurs français
- KwdFr :
- Chromatographie sur gel (MeSH), Cinétique (MeSH), Dimérisation (MeSH), Disulfures (composition chimique), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Modèles moléculaires (MeSH), Saccharomyces cerevisiae (composition chimique), Structure quaternaire des protéines (MeSH), Éthanol (analogues et dérivés), Éthanol (composition chimique).
- MESH :
- analogues et dérivés : Éthanol.
- composition chimique : Disulfures, Glutarédoxines, Saccharomyces cerevisiae, Éthanol.
- métabolisme : Glutarédoxines.
- Chromatographie sur gel, Cinétique, Dimérisation, Modèles moléculaires, Structure quaternaire des protéines.
English descriptors
- KwdEn :
- Chromatography, Gel (MeSH), Dimerization (MeSH), Disulfides (chemistry), Ethanol (analogs & derivatives), Ethanol (chemistry), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Kinetics (MeSH), Models, Molecular (MeSH), Protein Structure, Quaternary (MeSH), Saccharomyces cerevisiae (chemistry).
- MESH :
- chemical , analogs & derivatives : Ethanol.
- chemical , chemistry : Disulfides, Ethanol, Glutaredoxins.
- chemical , metabolism : Glutaredoxins.
- chemistry : Saccharomyces cerevisiae.
- Chromatography, Gel, Dimerization, Kinetics, Models, Molecular, Protein Structure, Quaternary.
Abstract
Two novel monothiol glutaredoxins from yeast (ScGrx6 and ScGrx7) were identified and analyzed in vitro. Both proteins are highly suited to study structure-function relationships of glutaredoxin subclasses because they differ from all monothiol glutaredoxins investigated so far and share features with dithiol glutaredoxins. ScGrx6 and ScGrx7 are, for example, the first monothiol glutaredoxins showing an activity in the standard glutaredoxin transhydrogenase assay with glutathione and bis-(2-hydroxyethyl)-disulfide. Steady-state kinetics of ScGrx7 with glutathione and cysteine-glutathione disulfide are similar to dithiol glutaredoxins and are consistent with a ping-pong mechanism. In contrast to most other glutaredoxins, ScGrx7 and ScGrx6 are able to dimerize noncovalently. Furthermore, ScGrx6 is the first monothiol glutaredoxin shown to directly bind an iron-sulfur cluster. The cluster can be stabilized by reduced glutathione, and its loss results in the conversion of tetramers to dimers. ScGrx7 does not bind metal ions but can be covalently modified in Escherichia coli leading to a mass shift of 1090 +/- 14 Da. What might be the structural requirements that cause the different properties? We hypothesize that a G(S/T)x3 insertion between a highly conserved lysine residue and the active site cysteine residue could be responsible for the abrogated transhydrogenase activity of many monothiol glutaredoxins. In addition, we suggest an active site motif without proline residues that could lead to the identification of further metal binding glutaredoxins. Such different properties presumably reflect diverse functions in vivo and might therefore explain why there are at least seven glutaredoxins in yeast.
DOI: 10.1021/bi7017865
PubMed: 18171082
Affiliations:
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Le document en format XML
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Herrmann</name></author><author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name></author></analytic><series><title level="j">Biochemistry</title><idno type="ISSN">0006-2960</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Chromatography, Gel (MeSH)</term><term>Dimerization (MeSH)</term><term>Disulfides (chemistry)</term><term>Ethanol (analogs & derivatives)</term><term>Ethanol (chemistry)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (metabolism)</term><term>Kinetics (MeSH)</term><term>Models, Molecular (MeSH)</term><term>Protein Structure, Quaternary (MeSH)</term><term>Saccharomyces cerevisiae (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Chromatographie sur gel (MeSH)</term><term>Cinétique (MeSH)</term><term>Dimérisation (MeSH)</term><term>Disulfures (composition chimique)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (métabolisme)</term><term>Modèles moléculaires (MeSH)</term><term>Saccharomyces cerevisiae (composition chimique)</term><term>Structure quaternaire des protéines (MeSH)</term><term>Éthanol (analogues et dérivés)</term><term>Éthanol (composition chimique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Ethanol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Disulfides</term><term>Ethanol</term><term>Glutaredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Éthanol</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Disulfures</term><term>Glutarédoxines</term><term>Saccharomyces cerevisiae</term><term>Éthanol</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, Gel</term><term>Dimerization</term><term>Kinetics</term><term>Models, Molecular</term><term>Protein Structure, Quaternary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie sur gel</term><term>Cinétique</term><term>Dimérisation</term><term>Modèles moléculaires</term><term>Structure quaternaire des protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Two novel monothiol glutaredoxins from yeast (ScGrx6 and ScGrx7) were identified and analyzed in vitro. Both proteins are highly suited to study structure-function relationships of glutaredoxin subclasses because they differ from all monothiol glutaredoxins investigated so far and share features with dithiol glutaredoxins. ScGrx6 and ScGrx7 are, for example, the first monothiol glutaredoxins showing an activity in the standard glutaredoxin transhydrogenase assay with glutathione and bis-(2-hydroxyethyl)-disulfide. Steady-state kinetics of ScGrx7 with glutathione and cysteine-glutathione disulfide are similar to dithiol glutaredoxins and are consistent with a ping-pong mechanism. In contrast to most other glutaredoxins, ScGrx7 and ScGrx6 are able to dimerize noncovalently. Furthermore, ScGrx6 is the first monothiol glutaredoxin shown to directly bind an iron-sulfur cluster. The cluster can be stabilized by reduced glutathione, and its loss results in the conversion of tetramers to dimers. ScGrx7 does not bind metal ions but can be covalently modified in Escherichia coli leading to a mass shift of 1090 +/- 14 Da. What might be the structural requirements that cause the different properties? We hypothesize that a G(S/T)x3 insertion between a highly conserved lysine residue and the active site cysteine residue could be responsible for the abrogated transhydrogenase activity of many monothiol glutaredoxins. In addition, we suggest an active site motif without proline residues that could lead to the identification of further metal binding glutaredoxins. Such different properties presumably reflect diverse functions in vivo and might therefore explain why there are at least seven glutaredoxins in yeast.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18171082</PMID><DateCompleted><Year>2008</Year><Month>03</Month><Day>20</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>47</Volume><Issue>5</Issue><PubDate><Year>2008</Year><Month>Feb</Month><Day>05</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Two novel monothiol glutaredoxins from Saccharomyces cerevisiae provide further insight into iron-sulfur cluster binding, oligomerization, and enzymatic activity of glutaredoxins.</ArticleTitle><Pagination><MedlinePgn>1452-63</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/bi7017865</ELocationID><Abstract><AbstractText>Two novel monothiol glutaredoxins from yeast (ScGrx6 and ScGrx7) were identified and analyzed in vitro. Both proteins are highly suited to study structure-function relationships of glutaredoxin subclasses because they differ from all monothiol glutaredoxins investigated so far and share features with dithiol glutaredoxins. ScGrx6 and ScGrx7 are, for example, the first monothiol glutaredoxins showing an activity in the standard glutaredoxin transhydrogenase assay with glutathione and bis-(2-hydroxyethyl)-disulfide. Steady-state kinetics of ScGrx7 with glutathione and cysteine-glutathione disulfide are similar to dithiol glutaredoxins and are consistent with a ping-pong mechanism. In contrast to most other glutaredoxins, ScGrx7 and ScGrx6 are able to dimerize noncovalently. Furthermore, ScGrx6 is the first monothiol glutaredoxin shown to directly bind an iron-sulfur cluster. The cluster can be stabilized by reduced glutathione, and its loss results in the conversion of tetramers to dimers. ScGrx7 does not bind metal ions but can be covalently modified in Escherichia coli leading to a mass shift of 1090 +/- 14 Da. What might be the structural requirements that cause the different properties? We hypothesize that a G(S/T)x3 insertion between a highly conserved lysine residue and the active site cysteine residue could be responsible for the abrogated transhydrogenase activity of many monothiol glutaredoxins. In addition, we suggest an active site motif without proline residues that could lead to the identification of further metal binding glutaredoxins. Such different properties presumably reflect diverse functions in vivo and might therefore explain why there are at least seven glutaredoxins in yeast.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mesecke</LastName><ForeName>Nikola</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Adolf-Butenandt-Institut für Physiologische Chemie, Ludwig-Maximilians Universität D-81377, München, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mittler</LastName><ForeName>Sarah</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Eckers</LastName><ForeName>Elisabeth</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Herrmann</LastName><ForeName>Johannes M</ForeName><Initials>JM</Initials></Author><Author ValidYN="Y"><LastName>Deponte</LastName><ForeName>Marcel</ForeName><Initials>M</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>2008</Year><Month>01</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3K9958V90M</RegistryNumber><NameOfSubstance UI="D000431">Ethanol</NameOfSubstance></Chemical><Chemical><RegistryNumber>45543L74BS</RegistryNumber><NameOfSubstance UI="C031319">2-hydroxyethyl disulfide</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002850" MajorTopicYN="N">Chromatography, Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019281" MajorTopicYN="N">Dimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000431" MajorTopicYN="N">Ethanol</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020836" MajorTopicYN="N">Protein Structure, Quaternary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>1</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>3</Month><Day>21</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>1</Month><Day>4</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18171082</ArticleId><ArticleId IdType="doi">10.1021/bi7017865</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bavière</li><li>District de Haute-Bavière</li></region><settlement><li>Munich</li></settlement></list><tree><noCountry><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name><name sortKey="Eckers, Elisabeth" sort="Eckers, Elisabeth" uniqKey="Eckers E" first="Elisabeth" last="Eckers">Elisabeth Eckers</name><name sortKey="Herrmann, Johannes M" sort="Herrmann, Johannes M" uniqKey="Herrmann J" first="Johannes M" last="Herrmann">Johannes M. Herrmann</name><name sortKey="Mittler, Sarah" sort="Mittler, Sarah" uniqKey="Mittler S" first="Sarah" last="Mittler">Sarah Mittler</name></noCountry><country name="Allemagne"><region name="Bavière"><name sortKey="Mesecke, Nikola" sort="Mesecke, Nikola" uniqKey="Mesecke N" first="Nikola" last="Mesecke">Nikola Mesecke</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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