The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology.
Identifieur interne : 000502 ( Main/Exploration ); précédent : 000501; suivant : 000503The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology.
Auteurs : Lefentse N. Mashamaite [Afrique du Sud] ; Johann M. Rohwer [Afrique du Sud] ; Ché S. Pillay [Afrique du Sud]Source :
- Bioscience reports [ 1573-4935 ] ; 2015.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Glutaredoxins, Saccharomyces cerevisiae Proteins, Sulfhydryl Compounds.
- metabolism : Saccharomyces cerevisiae.
- Humans, Kinetics, Models, Biological, Oxidation-Reduction, Systems Biology.
Abstract
Glutathionylation plays a central role in cellular redox regulation and anti-oxidative defence. Grx (Glutaredoxins) are primarily responsible for reversing glutathionylation and their activity therefore affects a range of cellular processes, making them prime candidates for computational systems biology studies. However, two distinct kinetic mechanisms involving either one (monothiol) or both (dithiol) active-site cysteines have been proposed for their deglutathionylation activity and initial studies predicted that computational models based on either of these mechanisms will have different structural and kinetic properties. Further, a number of other discrepancies including the relative activity of active-site mutants and contrasting reciprocal plot kinetics have also been reported for these redoxins. Using kinetic modelling, we show that the dithiol and monothiol mechanisms are identical and, we were also able to explain much of the discrepant data found within the literature on Grx activity and kinetics. Moreover, our results have revealed how an apparently futile side-reaction in the monothiol mechanism may play a significant role in regulating Grx activity in vivo.
DOI: 10.1042/BSR20140157
PubMed: 25514238
PubMed Central: PMC4340274
Affiliations:
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Rohwer</name><affiliation wicri:level="1"><nlm:affiliation>†Department of Biochemistry, Stellenbosch University, Private Bag X1, Matieland, 7602 Stellenbosch, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>†Department of Biochemistry, Stellenbosch University, Private Bag X1, Matieland, 7602 Stellenbosch</wicri:regionArea><wicri:noRegion>7602 Stellenbosch</wicri:noRegion></affiliation></author><author><name sortKey="Pillay, Che S" sort="Pillay, Che S" uniqKey="Pillay C" first="Ché S" last="Pillay">Ché S. Pillay</name><affiliation wicri:level="1"><nlm:affiliation>*School of Life Sciences, University of KwaZulu-Natal, Carbis Road, Pietermaritzburg, 3201, South Africa.</nlm:affiliation><country xml:lang="fr">Afrique du Sud</country><wicri:regionArea>*School of Life Sciences, University of KwaZulu-Natal, Carbis Road, Pietermaritzburg, 3201</wicri:regionArea><wicri:noRegion>3201</wicri:noRegion></affiliation></author></analytic><series><title level="j">Bioscience reports</title><idno type="eISSN">1573-4935</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Glutaredoxins (metabolism)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Models, Biological (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Systems Biology (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biologie des systèmes (MeSH)</term><term>Cinétique (MeSH)</term><term>Glutarédoxines (métabolisme)</term><term>Humains (MeSH)</term><term>Modèles biologiques (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Thiols (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Saccharomyces cerevisiae Proteins</term><term>Sulfhydryl Compounds</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term><term>Thiols</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Kinetics</term><term>Models, Biological</term><term>Oxidation-Reduction</term><term>Systems Biology</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biologie des systèmes</term><term>Cinétique</term><term>Humains</term><term>Modèles biologiques</term><term>Oxydoréduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutathionylation plays a central role in cellular redox regulation and anti-oxidative defence. Grx (Glutaredoxins) are primarily responsible for reversing glutathionylation and their activity therefore affects a range of cellular processes, making them prime candidates for computational systems biology studies. However, two distinct kinetic mechanisms involving either one (monothiol) or both (dithiol) active-site cysteines have been proposed for their deglutathionylation activity and initial studies predicted that computational models based on either of these mechanisms will have different structural and kinetic properties. Further, a number of other discrepancies including the relative activity of active-site mutants and contrasting reciprocal plot kinetics have also been reported for these redoxins. Using kinetic modelling, we show that the dithiol and monothiol mechanisms are identical and, we were also able to explain much of the discrepant data found within the literature on Grx activity and kinetics. Moreover, our results have revealed how an apparently futile side-reaction in the monothiol mechanism may play a significant role in regulating Grx activity in vivo.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25514238</PMID><DateCompleted><Year>2015</Year><Month>12</Month><Day>14</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1573-4935</ISSN><JournalIssue CitedMedium="Internet"><Volume>35</Volume><Issue>1</Issue><PubDate><Year>2015</Year><Month>Feb</Month><Day>25</Day></PubDate></JournalIssue><Title>Bioscience reports</Title><ISOAbbreviation>Biosci Rep</ISOAbbreviation></Journal><ArticleTitle>The glutaredoxin mono- and di-thiol mechanisms for deglutathionylation are functionally equivalent: implications for redox systems biology.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1042/BSR20140157</ELocationID><ELocationID EIdType="pii" ValidYN="Y">e00173</ELocationID><Abstract><AbstractText>Glutathionylation plays a central role in cellular redox regulation and anti-oxidative defence. Grx (Glutaredoxins) are primarily responsible for reversing glutathionylation and their activity therefore affects a range of cellular processes, making them prime candidates for computational systems biology studies. However, two distinct kinetic mechanisms involving either one (monothiol) or both (dithiol) active-site cysteines have been proposed for their deglutathionylation activity and initial studies predicted that computational models based on either of these mechanisms will have different structural and kinetic properties. Further, a number of other discrepancies including the relative activity of active-site mutants and contrasting reciprocal plot kinetics have also been reported for these redoxins. Using kinetic modelling, we show that the dithiol and monothiol mechanisms are identical and, we were also able to explain much of the discrepant data found within the literature on Grx activity and kinetics. Moreover, our results have revealed how an apparently futile side-reaction in the monothiol mechanism may play a significant role in regulating Grx activity in vivo.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mashamaite</LastName><ForeName>Lefentse N</ForeName><Initials>LN</Initials><AffiliationInfo><Affiliation>*School of Life Sciences, University of KwaZulu-Natal, Carbis Road, Pietermaritzburg, 3201, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rohwer</LastName><ForeName>Johann M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>†Department of Biochemistry, Stellenbosch University, Private Bag X1, Matieland, 7602 Stellenbosch, South Africa.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pillay</LastName><ForeName>Ché S</ForeName><Initials>CS</Initials><AffiliationInfo><Affiliation>*School of Life Sciences, University of KwaZulu-Natal, Carbis Road, Pietermaritzburg, 3201, South Africa.</Affiliation></AffiliationInfo></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>2015</Year><Month>02</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biosci Rep</MedlineTA><NlmUniqueID>8102797</NlmUniqueID><ISSNLinking>0144-8463</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl 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Mashamaite</name></noRegion><name sortKey="Pillay, Che S" sort="Pillay, Che S" uniqKey="Pillay C" first="Ché S" last="Pillay">Ché S. Pillay</name><name sortKey="Rohwer, Johann M" sort="Rohwer, Johann M" uniqKey="Rohwer J" first="Johann M" last="Rohwer">Johann M. Rohwer</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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