Biochemical and thermodynamic comparison of the selenocysteine containing and non-containing thioredoxin glutathione reductase of Fasciola gigantica.
Identifieur interne : 000288 ( Main/Exploration ); précédent : 000287; suivant : 000289Biochemical and thermodynamic comparison of the selenocysteine containing and non-containing thioredoxin glutathione reductase of Fasciola gigantica.
Auteurs : Parismita Kalita [Inde] ; Harish Shukla [Inde] ; Rohit Shukla [Inde] ; Timir Tripathi [Inde]Source :
- Biochimica et biophysica acta. General subjects [ 0304-4165 ] ; 2018.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Bovins (MeSH), Complexes multienzymatiques (composition chimique), Complexes multienzymatiques (isolement et purification), Complexes multienzymatiques (métabolisme), Fasciola (enzymologie), Foie (enzymologie), Foie (parasitologie), Glutathion (métabolisme), Liaison aux protéines (MeSH), Modèles moléculaires (MeSH), NADH, NADPH oxidoreductases (composition chimique), NADH, NADPH oxidoreductases (isolement et purification), NADH, NADPH oxidoreductases (métabolisme), Oxydoréduction (MeSH), Simulation de docking moléculaire (MeSH), Sites de fixation (MeSH), Sélénocystéine (composition chimique), Sélénocystéine (métabolisme), Thermodynamique (MeSH).
- MESH :
- composition chimique : Complexes multienzymatiques, NADH, NADPH oxidoreductases, Sélénocystéine.
- enzymologie : Fasciola, Foie.
- isolement et purification : Complexes multienzymatiques, NADH, NADPH oxidoreductases.
- métabolisme : Complexes multienzymatiques, Glutathion, NADH, NADPH oxidoreductases, Sélénocystéine.
- parasitologie : Foie.
- Animaux, Bovins, Liaison aux protéines, Modèles moléculaires, Oxydoréduction, Simulation de docking moléculaire, Sites de fixation, Thermodynamique.
English descriptors
- KwdEn :
- Animals (MeSH), Binding Sites (MeSH), Cattle (MeSH), Fasciola (enzymology), Glutathione (metabolism), Liver (enzymology), Liver (parasitology), Models, Molecular (MeSH), Molecular Docking Simulation (MeSH), Multienzyme Complexes (chemistry), Multienzyme Complexes (isolation & purification), Multienzyme Complexes (metabolism), NADH, NADPH Oxidoreductases (chemistry), NADH, NADPH Oxidoreductases (isolation & purification), NADH, NADPH Oxidoreductases (metabolism), Oxidation-Reduction (MeSH), Protein Binding (MeSH), Selenocysteine (chemistry), Selenocysteine (metabolism), Thermodynamics (MeSH).
- MESH :
- chemical , chemistry : Multienzyme Complexes, NADH, NADPH Oxidoreductases, Selenocysteine.
- chemical , isolation & purification : Multienzyme Complexes, NADH, NADPH Oxidoreductases.
- chemical , metabolism : Glutathione, Multienzyme Complexes, NADH, NADPH Oxidoreductases, Selenocysteine.
- enzymology : Fasciola, Liver.
- parasitology : Liver.
- Animals, Binding Sites, Cattle, Models, Molecular, Molecular Docking Simulation, Oxidation-Reduction, Protein Binding, Thermodynamics.
Abstract
The thiol-disulfide redox metabolism in platyhelminth parasites depends entirely on a single selenocysteine (Sec) containing flavoenzyme, thioredoxin glutathione reductase (TGR) that links the classical thioredoxin (Trx) and glutathione (GSH) systems. In the present study, we investigated the catalytic and structural properties of different variants of Fasciola gigantica TGR to understand the role of Sec. The recombinant full-length Sec containing TGR (FgTGRsec), TGR without Sec (FgTGR) and TGRsec without the N-terminal glutaredoxin (Grx) domain (∆NTD-FgTGRsec) were purified to homogeneity. Biochemical studies revealed that Sec597 is responsible for higher thioredoxin reductase (TrxR) and glutathione reductase (GR) activity of FgTGRsec. The N-terminal Grx domain was found to positively regulate the DTNB-based TrxR activity of FgTGRsec. The FgTGRsec was highly sensitive to inhibition by auranofin (AF). The structure of FgTGR was modeled, and the inhibitor AF was docked, and binding sites were identified. Unfolding studies suggest that all three proteins are highly cooperative molecules since during GdnHCl-induced denaturation, a monophasic unfolding of the proteins without stabilization of any intermediate is observed. The Cm for GdnHCl induced unfolding of FgTGR was higher than FgTGRsec and ∆NTD-FgTGRsec suggesting that FgTGR without Sec was more stable in solution than the other protein variants. The free energy of stabilization for the proteins was also determined. To our knowledge, this is also the first report on unfolding and stability analysis of any TGR.
DOI: 10.1016/j.bbagen.2018.03.007
PubMed: 29526505
Affiliations:
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Electronic address: ttripathi@nehu.ac.in.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022</wicri:regionArea><wicri:noRegion>Shillong 793022</wicri:noRegion></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. General subjects</title><idno type="ISSN">0304-4165</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Binding Sites (MeSH)</term><term>Cattle (MeSH)</term><term>Fasciola (enzymology)</term><term>Glutathione (metabolism)</term><term>Liver (enzymology)</term><term>Liver (parasitology)</term><term>Models, Molecular (MeSH)</term><term>Molecular Docking Simulation (MeSH)</term><term>Multienzyme Complexes (chemistry)</term><term>Multienzyme Complexes (isolation & purification)</term><term>Multienzyme Complexes (metabolism)</term><term>NADH, NADPH Oxidoreductases (chemistry)</term><term>NADH, NADPH Oxidoreductases (isolation & purification)</term><term>NADH, NADPH Oxidoreductases (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Protein Binding (MeSH)</term><term>Selenocysteine (chemistry)</term><term>Selenocysteine (metabolism)</term><term>Thermodynamics (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Bovins (MeSH)</term><term>Complexes multienzymatiques (composition chimique)</term><term>Complexes multienzymatiques (isolement et purification)</term><term>Complexes multienzymatiques (métabolisme)</term><term>Fasciola (enzymologie)</term><term>Foie (enzymologie)</term><term>Foie (parasitologie)</term><term>Glutathion (métabolisme)</term><term>Liaison aux protéines (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>NADH, NADPH oxidoreductases (composition chimique)</term><term>NADH, NADPH oxidoreductases (isolement et purification)</term><term>NADH, NADPH oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Simulation de docking moléculaire (MeSH)</term><term>Sites de fixation (MeSH)</term><term>Sélénocystéine (composition chimique)</term><term>Sélénocystéine (métabolisme)</term><term>Thermodynamique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Selenocysteine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutathione</term><term>Multienzyme Complexes</term><term>NADH, NADPH Oxidoreductases</term><term>Selenocysteine</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Complexes multienzymatiques</term><term>NADH, NADPH oxidoreductases</term><term>Sélénocystéine</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Fasciola</term><term>Foie</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fasciola</term><term>Liver</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Complexes multienzymatiques</term><term>NADH, NADPH oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexes multienzymatiques</term><term>Glutathion</term><term>NADH, NADPH oxidoreductases</term><term>Sélénocystéine</term></keywords><keywords scheme="MESH" qualifier="parasitologie" xml:lang="fr"><term>Foie</term></keywords><keywords scheme="MESH" qualifier="parasitology" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Binding Sites</term><term>Cattle</term><term>Models, Molecular</term><term>Molecular Docking Simulation</term><term>Oxidation-Reduction</term><term>Protein Binding</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Bovins</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Oxydoréduction</term><term>Simulation de docking moléculaire</term><term>Sites de fixation</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The thiol-disulfide redox metabolism in platyhelminth parasites depends entirely on a single selenocysteine (Sec) containing flavoenzyme, thioredoxin glutathione reductase (TGR) that links the classical thioredoxin (Trx) and glutathione (GSH) systems. In the present study, we investigated the catalytic and structural properties of different variants of Fasciola gigantica TGR to understand the role of Sec. The recombinant full-length Sec containing TGR (FgTGRsec), TGR without Sec (FgTGR) and TGRsec without the N-terminal glutaredoxin (Grx) domain (∆NTD-FgTGRsec) were purified to homogeneity. Biochemical studies revealed that Sec597 is responsible for higher thioredoxin reductase (TrxR) and glutathione reductase (GR) activity of FgTGRsec. The N-terminal Grx domain was found to positively regulate the DTNB-based TrxR activity of FgTGRsec. The FgTGRsec was highly sensitive to inhibition by auranofin (AF). The structure of FgTGR was modeled, and the inhibitor AF was docked, and binding sites were identified. Unfolding studies suggest that all three proteins are highly cooperative molecules since during GdnHCl-induced denaturation, a monophasic unfolding of the proteins without stabilization of any intermediate is observed. The Cm for GdnHCl induced unfolding of FgTGR was higher than FgTGRsec and ∆NTD-FgTGRsec suggesting that FgTGR without Sec was more stable in solution than the other protein variants. The free energy of stabilization for the proteins was also determined. To our knowledge, this is also the first report on unfolding and stability analysis of any TGR.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29526505</PMID><DateCompleted><Year>2018</Year><Month>11</Month><Day>06</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>06</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0304-4165</ISSN><JournalIssue CitedMedium="Print"><Volume>1862</Volume><Issue>6</Issue><PubDate><Year>2018</Year><Month>06</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta. General subjects</Title><ISOAbbreviation>Biochim Biophys Acta Gen Subj</ISOAbbreviation></Journal><ArticleTitle>Biochemical and thermodynamic comparison of the selenocysteine containing and non-containing thioredoxin glutathione reductase of Fasciola gigantica.</ArticleTitle><Pagination><MedlinePgn>1306-1316</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(18)30063-1</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2018.03.007</ELocationID><Abstract><AbstractText>The thiol-disulfide redox metabolism in platyhelminth parasites depends entirely on a single selenocysteine (Sec) containing flavoenzyme, thioredoxin glutathione reductase (TGR) that links the classical thioredoxin (Trx) and glutathione (GSH) systems. In the present study, we investigated the catalytic and structural properties of different variants of Fasciola gigantica TGR to understand the role of Sec. The recombinant full-length Sec containing TGR (FgTGRsec), TGR without Sec (FgTGR) and TGRsec without the N-terminal glutaredoxin (Grx) domain (∆NTD-FgTGRsec) were purified to homogeneity. Biochemical studies revealed that Sec597 is responsible for higher thioredoxin reductase (TrxR) and glutathione reductase (GR) activity of FgTGRsec. The N-terminal Grx domain was found to positively regulate the DTNB-based TrxR activity of FgTGRsec. The FgTGRsec was highly sensitive to inhibition by auranofin (AF). The structure of FgTGR was modeled, and the inhibitor AF was docked, and binding sites were identified. Unfolding studies suggest that all three proteins are highly cooperative molecules since during GdnHCl-induced denaturation, a monophasic unfolding of the proteins without stabilization of any intermediate is observed. The Cm for GdnHCl induced unfolding of FgTGR was higher than FgTGRsec and ∆NTD-FgTGRsec suggesting that FgTGR without Sec was more stable in solution than the other protein variants. The free energy of stabilization for the proteins was also determined. To our knowledge, this is also the first report on unfolding and stability analysis of any TGR.</AbstractText><CopyrightInformation>Copyright © 2018 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kalita</LastName><ForeName>Parismita</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shukla</LastName><ForeName>Harish</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shukla</LastName><ForeName>Rohit</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tripathi</LastName><ForeName>Timir</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong 793022, India. Electronic address: ttripathi@nehu.ac.in.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>03</Month><Day>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Gen Subj</MedlineTA><NlmUniqueID>101731726</NlmUniqueID><ISSNLinking>0304-4165</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0CH9049VIS</RegistryNumber><NameOfSubstance UI="D017279">Selenocysteine</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.-</RegistryNumber><NameOfSubstance UI="D009247">NADH, NADPH Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.4.-</RegistryNumber><NameOfSubstance UI="C466433">thioredoxin glutathione reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005209" MajorTopicYN="N">Fasciola</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000469" MajorTopicYN="Y">parasitology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D062105" MajorTopicYN="N">Molecular Docking Simulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="N">Multienzyme Complexes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009247" MajorTopicYN="N">NADH, NADPH Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017279" MajorTopicYN="N">Selenocysteine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013816" MajorTopicYN="N">Thermodynamics</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Activity</Keyword><Keyword MajorTopicYN="Y">Auranofin</Keyword><Keyword MajorTopicYN="Y">Glutathione</Keyword><Keyword MajorTopicYN="Y">Glutathione reductase</Keyword><Keyword MajorTopicYN="Y">Homology modeling</Keyword><Keyword MajorTopicYN="Y">Inhibition</Keyword><Keyword MajorTopicYN="Y">Liver fluke</Keyword><Keyword MajorTopicYN="Y">Parasite</Keyword><Keyword MajorTopicYN="Y">Platyhelminthes</Keyword><Keyword MajorTopicYN="Y">Thioredoxin glutathione reductase</Keyword><Keyword MajorTopicYN="Y">Thioredoxin reductase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>11</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>03</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>03</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>3</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>11</Month><Day>7</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>3</Month><Day>13</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29526505</ArticleId><ArticleId IdType="pii">S0304-4165(18)30063-1</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2018.03.007</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Kalita, Parismita" sort="Kalita, Parismita" uniqKey="Kalita P" first="Parismita" last="Kalita">Parismita Kalita</name></noRegion><name sortKey="Shukla, Harish" sort="Shukla, Harish" uniqKey="Shukla H" first="Harish" last="Shukla">Harish Shukla</name><name sortKey="Shukla, Rohit" sort="Shukla, Rohit" uniqKey="Shukla R" first="Rohit" last="Shukla">Rohit Shukla</name><name sortKey="Tripathi, Timir" sort="Tripathi, Timir" uniqKey="Tripathi T" first="Timir" last="Tripathi">Timir 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