Purification and characterization of two-domain glutaredoxin in the parasitic helminth Fasciola gigantica.
Identifieur interne : 000326 ( Main/Exploration ); précédent : 000325; suivant : 000327Purification and characterization of two-domain glutaredoxin in the parasitic helminth Fasciola gigantica.
Auteurs : Ankita Gupta [Inde] ; Banchob Sripa [Thaïlande] ; Timir Tripathi [Inde]Source :
- Parasitology international [ 1873-0329 ] ; 2017.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Escherichia coli (génétique), Expression des gènes (MeSH), Fasciola (génétique), Fasciola (physiologie), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Organismes génétiquement modifiés (MeSH), Protéines d'helminthes (composition chimique), Protéines d'helminthes (génétique), Protéines d'helminthes (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Protéines d'helminthes.
- génétique : Escherichia coli, Fasciola, Glutarédoxines, Protéines d'helminthes, Protéines recombinantes.
- métabolisme : Glutarédoxines, Protéines d'helminthes, Protéines recombinantes.
- physiologie : Fasciola.
- Alignement de séquences, Animaux, Expression des gènes, Organismes génétiquement modifiés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Escherichia coli (genetics), Fasciola (genetics), Fasciola (physiology), Gene Expression (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Helminth Proteins (chemistry), Helminth Proteins (genetics), Helminth Proteins (metabolism), Organisms, Genetically Modified (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH).
- MESH :
- chemical , chemistry : Glutaredoxins, Helminth Proteins.
- genetics : Escherichia coli, Fasciola, Glutaredoxins, Helminth Proteins, Recombinant Proteins.
- chemical , metabolism : Glutaredoxins, Helminth Proteins, Recombinant Proteins.
- physiology : Fasciola.
- Amino Acid Sequence, Animals, Gene Expression, Organisms, Genetically Modified, Sequence Alignment.
Abstract
Glutaredoxins (Grxs) are small thiol-dependent proteins and key elements of redox signaling as they regulate the redox state of important cellular proteins. In the present study, the complete sequence of a glutaredoxin protein, obtained from the liver fluke Fasciola gigantica, was PCR-amplified and cloned. The 690-bp open reading frame (ORF) encodes a 230-amino acid protein with two conserved domains (FgGrxD1 and FgGrxD2) and has similarities with two monothiol Grxs of Saccharomyces cerevisiae, i.e., ScGrx3 and ScGrx4. The full-length FgGrx along with its two constituent domains were overexpressed in Escherichia coli as hexahistidyl-tagged proteins. The affinity chromatography resulted in almost pure and soluble proteins. The full-length FgGrx and the FgGrxD2 showed reddish-brown color, indicating the presence of bound iron in the second domain. In the insulin based reduction assay, both FgGrx and FgGrxD2 containing the active site motif CGFS exhibited a weak reducing activity, whereas FgGrxD1 was inactive. Additionally, FgGrx did not show any GSH-disulfide transhydrogenase activity when 2-hydroxyethyl disulfide (HED) or de-hydroascorbate (DHA) were taken as substrates. These results indicated the probable role of FgGrx in cellular iron-sulfur homeostasis. FgGrx was found to be reversibly S-glutathionylated, suggesting a potential redox regulation that is likely to take place at the active site Cys158. Since there is only one Cys in FgGrxD2, the Cys158 might be involved in FeS binding. This study is the first report on the presence of Grx in platyhelminthic parasites and provides a starting point for further characterization of the redox network in liver flukes.
DOI: 10.1016/j.parint.2016.05.005
PubMed: 27189489
Affiliations:
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Electronic address: timir.tripathi@gmail.com.</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">Parasitology international</title><idno type="eISSN">1873-0329</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Escherichia coli (genetics)</term><term>Fasciola (genetics)</term><term>Fasciola (physiology)</term><term>Gene Expression (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Helminth Proteins (chemistry)</term><term>Helminth Proteins (genetics)</term><term>Helminth Proteins (metabolism)</term><term>Organisms, Genetically Modified (MeSH)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Sequence Alignment (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term><term>Animaux (MeSH)</term><term>Escherichia coli (génétique)</term><term>Expression des gènes (MeSH)</term><term>Fasciola (génétique)</term><term>Fasciola (physiologie)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Organismes génétiquement modifiés (MeSH)</term><term>Protéines d'helminthes (composition chimique)</term><term>Protéines d'helminthes (génétique)</term><term>Protéines d'helminthes (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Helminth Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines d'helminthes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Fasciola</term><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Fasciola</term><term>Glutarédoxines</term><term>Protéines d'helminthes</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Helminth Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Protéines d'helminthes</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Fasciola</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Fasciola</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Gene Expression</term><term>Organisms, Genetically Modified</term><term>Sequence Alignment</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Alignement de séquences</term><term>Animaux</term><term>Expression des gènes</term><term>Organismes génétiquement modifiés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are small thiol-dependent proteins and key elements of redox signaling as they regulate the redox state of important cellular proteins. In the present study, the complete sequence of a glutaredoxin protein, obtained from the liver fluke Fasciola gigantica, was PCR-amplified and cloned. The 690-bp open reading frame (ORF) encodes a 230-amino acid protein with two conserved domains (FgGrxD1 and FgGrxD2) and has similarities with two monothiol Grxs of Saccharomyces cerevisiae, i.e., ScGrx3 and ScGrx4. The full-length FgGrx along with its two constituent domains were overexpressed in Escherichia coli as hexahistidyl-tagged proteins. The affinity chromatography resulted in almost pure and soluble proteins. The full-length FgGrx and the FgGrxD2 showed reddish-brown color, indicating the presence of bound iron in the second domain. In the insulin based reduction assay, both FgGrx and FgGrxD2 containing the active site motif CGFS exhibited a weak reducing activity, whereas FgGrxD1 was inactive. Additionally, FgGrx did not show any GSH-disulfide transhydrogenase activity when 2-hydroxyethyl disulfide (HED) or de-hydroascorbate (DHA) were taken as substrates. These results indicated the probable role of FgGrx in cellular iron-sulfur homeostasis. FgGrx was found to be reversibly S-glutathionylated, suggesting a potential redox regulation that is likely to take place at the active site Cys158. Since there is only one Cys in FgGrxD2, the Cys158 might be involved in FeS binding. This study is the first report on the presence of Grx in platyhelminthic parasites and provides a starting point for further characterization of the redox network in liver flukes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27189489</PMID><DateCompleted><Year>2018</Year><Month>03</Month><Day>21</Day></DateCompleted><DateRevised><Year>2018</Year><Month>03</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-0329</ISSN><JournalIssue CitedMedium="Internet"><Volume>66</Volume><Issue>4</Issue><PubDate><Year>2017</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Parasitology international</Title><ISOAbbreviation>Parasitol Int</ISOAbbreviation></Journal><ArticleTitle>Purification and characterization of two-domain glutaredoxin in the parasitic helminth Fasciola gigantica.</ArticleTitle><Pagination><MedlinePgn>432-435</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1383-5769(16)30119-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.parint.2016.05.005</ELocationID><Abstract><AbstractText>Glutaredoxins (Grxs) are small thiol-dependent proteins and key elements of redox signaling as they regulate the redox state of important cellular proteins. In the present study, the complete sequence of a glutaredoxin protein, obtained from the liver fluke Fasciola gigantica, was PCR-amplified and cloned. The 690-bp open reading frame (ORF) encodes a 230-amino acid protein with two conserved domains (FgGrxD1 and FgGrxD2) and has similarities with two monothiol Grxs of Saccharomyces cerevisiae, i.e., ScGrx3 and ScGrx4. The full-length FgGrx along with its two constituent domains were overexpressed in Escherichia coli as hexahistidyl-tagged proteins. The affinity chromatography resulted in almost pure and soluble proteins. The full-length FgGrx and the FgGrxD2 showed reddish-brown color, indicating the presence of bound iron in the second domain. In the insulin based reduction assay, both FgGrx and FgGrxD2 containing the active site motif CGFS exhibited a weak reducing activity, whereas FgGrxD1 was inactive. Additionally, FgGrx did not show any GSH-disulfide transhydrogenase activity when 2-hydroxyethyl disulfide (HED) or de-hydroascorbate (DHA) were taken as substrates. These results indicated the probable role of FgGrx in cellular iron-sulfur homeostasis. FgGrx was found to be reversibly S-glutathionylated, suggesting a potential redox regulation that is likely to take place at the active site Cys158. Since there is only one Cys in FgGrxD2, the Cys158 might be involved in FeS binding. This study is the first report on the presence of Grx in platyhelminthic parasites and provides a starting point for further characterization of the redox network in liver flukes.</AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Ireland Ltd. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Gupta</LastName><ForeName>Ankita</ForeName><Initials>A</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>Sripa</LastName><ForeName>Banchob</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Liver Fluke and Cholangiocarcinoma Research Center, Faculty of Medicine, Khon Kaen University, Khon Kaen, Thailand.</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: timir.tripathi@gmail.com.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>05</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Parasitol Int</MedlineTA><NlmUniqueID>9708549</NlmUniqueID><ISSNLinking>1383-5769</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015801">Helminth Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005209" MajorTopicYN="N">Fasciola</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015801" MajorTopicYN="N">Helminth Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D030781" MajorTopicYN="N">Organisms, Genetically Modified</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><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></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cysteine</Keyword><Keyword MajorTopicYN="N">Glutathionylation</Keyword><Keyword MajorTopicYN="N">Liver fluke</Keyword><Keyword MajorTopicYN="N">Redox</Keyword><Keyword MajorTopicYN="N">Thiol</Keyword><Keyword MajorTopicYN="N">Thioredoxin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>08</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>02</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>05</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>5</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>3</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>5</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27189489</ArticleId><ArticleId IdType="pii">S1383-5769(16)30119-2</ArticleId><ArticleId IdType="doi">10.1016/j.parint.2016.05.005</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li><li>Thaïlande</li></country></list><tree><country name="Inde"><noRegion><name sortKey="Gupta, Ankita" sort="Gupta, Ankita" uniqKey="Gupta A" first="Ankita" last="Gupta">Ankita Gupta</name></noRegion><name sortKey="Tripathi, Timir" sort="Tripathi, Timir" uniqKey="Tripathi T" first="Timir" last="Tripathi">Timir Tripathi</name></country><country name="Thaïlande"><noRegion><name sortKey="Sripa, Banchob" sort="Sripa, Banchob" uniqKey="Sripa B" first="Banchob" last="Sripa">Banchob Sripa</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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