Plasmodium falciparum antioxidant protein as a model enzyme for a special class of glutaredoxin/glutathione-dependent peroxiredoxins.
Identifieur interne : 000729 ( Main/Exploration ); précédent : 000728; suivant : 000730Plasmodium falciparum antioxidant protein as a model enzyme for a special class of glutaredoxin/glutathione-dependent peroxiredoxins.
Auteurs : Carine F. Djuika [Allemagne] ; Sabine Fiedler ; Martina Schnölzer ; Cecilia Sanchez ; Michael Lanzer ; Marcel DeponteSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2013.
Descripteurs français
- KwdFr :
- Antioxydants (composition chimique), Antioxydants (métabolisme), Catalyse (MeSH), Conformation des protéines (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (physiologie), Glutathion (physiologie), Multimérisation de protéines (MeSH), Oxydoréduction (MeSH), Peroxirédoxines (métabolisme), Plasmodium falciparum (enzymologie), Protéines de protozoaire (physiologie), Régulation allostérique (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : Antioxydants.
- enzymologie : Plasmodium falciparum.
- métabolisme : Antioxydants, Peroxirédoxines.
- physiologie : Glutarédoxines, Glutathion, Protéines de protozoaire.
- Catalyse, Conformation des protéines, Données de séquences moléculaires, Multimérisation de protéines, Oxydoréduction, Régulation allostérique, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Allosteric Regulation (MeSH), Amino Acid Sequence (MeSH), Antioxidants (chemistry), Antioxidants (metabolism), Catalysis (MeSH), Glutaredoxins (physiology), Glutathione (physiology), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Peroxiredoxins (metabolism), Plasmodium falciparum (enzymology), Protein Conformation (MeSH), Protein Multimerization (MeSH), Protozoan Proteins (physiology).
- MESH :
- chemical , chemistry : Antioxidants.
- chemical , metabolism : Antioxidants, Peroxiredoxins.
- chemical , physiology : Glutaredoxins, Glutathione, Protozoan Proteins.
- enzymology : Plasmodium falciparum.
- Allosteric Regulation, Amino Acid Sequence, Catalysis, Molecular Sequence Data, Oxidation-Reduction, Protein Conformation, Protein Multimerization.
Abstract
BACKGROUND
Peroxiredoxins are important heterogeneous thiol-dependent hydroperoxidases with a variety of isoforms and enzymatic mechanisms. A special subclass of glutaredoxin/glutathione-dependent peroxiredoxins has been discovered in bacteria and eukaryotes during the last decade, but the exact enzymatic mechanisms of these enzymes remain to be unraveled.
METHODS
We performed a comprehensive analysis of the enzyme kinetics and redox states of one of these glutaredoxin/glutathione-dependent peroxiredoxins, the antioxidant protein from the malaria parasite Plasmodium falciparum, using steady-state kinetic measurements, site-directed mutagenesis, redox mobility shift assays, gel filtration, and mass spectrometry.
RESULTS
P. falciparum antioxidant protein requires not only glutaredoxin but also glutathione as a true substrate for the reduction of hydroperoxides. One peroxiredoxin cysteine residue and one glutaredoxin cysteine residue are sufficient for catalysis, however, additional cysteine residues of both proteins result in alternative redox states and conformations in vitro with implications for redox regulation. Our data furthermore point to a glutathione-dependent peroxiredoxin activation and a negative subunit cooperativity.
CONCLUSIONS
The investigated glutaredoxin/glutathione/peroxiredoxin system provides numerous new insights into the mechanism and redox regulation of peroxiredoxins.
GENERAL SIGNIFICANCE
As a member of the special subclass of glutaredoxin/glutathione-dependent peroxiredoxins, the P. falciparum antioxidant protein could become a reference protein for peroxiredoxin catalysis and regulation.
DOI: 10.1016/j.bbagen.2013.04.020
PubMed: 23624334
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Djuika</name><affiliation wicri:level="3"><nlm:affiliation>Department of Parasitology, Ruprecht-Karls University, Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Parasitology, Ruprecht-Karls University, Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Fiedler, Sabine" sort="Fiedler, Sabine" uniqKey="Fiedler S" first="Sabine" last="Fiedler">Sabine Fiedler</name></author><author><name sortKey="Schnolzer, Martina" sort="Schnolzer, Martina" uniqKey="Schnolzer M" first="Martina" last="Schnölzer">Martina Schnölzer</name></author><author><name sortKey="Sanchez, Cecilia" sort="Sanchez, Cecilia" uniqKey="Sanchez C" first="Cecilia" last="Sanchez">Cecilia Sanchez</name></author><author><name sortKey="Lanzer, Michael" sort="Lanzer, Michael" uniqKey="Lanzer M" first="Michael" last="Lanzer">Michael Lanzer</name></author><author><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23624334</idno><idno type="pmid">23624334</idno><idno type="doi">10.1016/j.bbagen.2013.04.020</idno><idno type="wicri:Area/Main/Corpus">000743</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000743</idno><idno type="wicri:Area/Main/Curation">000743</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000743</idno><idno type="wicri:Area/Main/Exploration">000743</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Plasmodium falciparum antioxidant protein as a model enzyme for a special class of glutaredoxin/glutathione-dependent peroxiredoxins.</title><author><name sortKey="Djuika, Carine F" sort="Djuika, Carine F" uniqKey="Djuika C" first="Carine F" last="Djuika">Carine F. Djuika</name><affiliation wicri:level="3"><nlm:affiliation>Department of Parasitology, Ruprecht-Karls University, Heidelberg, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Parasitology, Ruprecht-Karls University, Heidelberg</wicri:regionArea><placeName><region type="land" nuts="1">Bade-Wurtemberg</region><region type="district" nuts="2">District de Karlsruhe</region><settlement type="city">Heidelberg</settlement></placeName></affiliation></author><author><name sortKey="Fiedler, Sabine" sort="Fiedler, Sabine" uniqKey="Fiedler S" first="Sabine" last="Fiedler">Sabine Fiedler</name></author><author><name sortKey="Schnolzer, Martina" sort="Schnolzer, Martina" uniqKey="Schnolzer M" first="Martina" last="Schnölzer">Martina Schnölzer</name></author><author><name sortKey="Sanchez, Cecilia" sort="Sanchez, Cecilia" uniqKey="Sanchez C" first="Cecilia" last="Sanchez">Cecilia Sanchez</name></author><author><name sortKey="Lanzer, Michael" sort="Lanzer, Michael" uniqKey="Lanzer M" first="Michael" last="Lanzer">Michael Lanzer</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">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Antioxidants (chemistry)</term><term>Antioxidants (metabolism)</term><term>Catalysis (MeSH)</term><term>Glutaredoxins (physiology)</term><term>Glutathione (physiology)</term><term>Molecular Sequence Data (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Peroxiredoxins (metabolism)</term><term>Plasmodium falciparum (enzymology)</term><term>Protein Conformation (MeSH)</term><term>Protein Multimerization (MeSH)</term><term>Protozoan Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antioxydants (composition chimique)</term><term>Antioxydants (métabolisme)</term><term>Catalyse (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Données de séquences moléculaires (MeSH)</term><term>Glutarédoxines (physiologie)</term><term>Glutathion (physiologie)</term><term>Multimérisation de protéines (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Peroxirédoxines (métabolisme)</term><term>Plasmodium falciparum (enzymologie)</term><term>Protéines de protozoaire (physiologie)</term><term>Régulation allostérique (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antioxidants</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>Peroxiredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Glutaredoxins</term><term>Glutathione</term><term>Protozoan Proteins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Antioxydants</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Plasmodium falciparum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term><term>Peroxirédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Glutarédoxines</term><term>Glutathion</term><term>Protéines de protozoaire</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term><term>Amino Acid Sequence</term><term>Catalysis</term><term>Molecular Sequence Data</term><term>Oxidation-Reduction</term><term>Protein Conformation</term><term>Protein Multimerization</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Conformation des protéines</term><term>Données de séquences moléculaires</term><term>Multimérisation de protéines</term><term>Oxydoréduction</term><term>Régulation allostérique</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Peroxiredoxins are important heterogeneous thiol-dependent hydroperoxidases with a variety of isoforms and enzymatic mechanisms. A special subclass of glutaredoxin/glutathione-dependent peroxiredoxins has been discovered in bacteria and eukaryotes during the last decade, but the exact enzymatic mechanisms of these enzymes remain to be unraveled.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>We performed a comprehensive analysis of the enzyme kinetics and redox states of one of these glutaredoxin/glutathione-dependent peroxiredoxins, the antioxidant protein from the malaria parasite Plasmodium falciparum, using steady-state kinetic measurements, site-directed mutagenesis, redox mobility shift assays, gel filtration, and mass spectrometry.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>P. falciparum antioxidant protein requires not only glutaredoxin but also glutathione as a true substrate for the reduction of hydroperoxides. One peroxiredoxin cysteine residue and one glutaredoxin cysteine residue are sufficient for catalysis, however, additional cysteine residues of both proteins result in alternative redox states and conformations in vitro with implications for redox regulation. Our data furthermore point to a glutathione-dependent peroxiredoxin activation and a negative subunit cooperativity.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>The investigated glutaredoxin/glutathione/peroxiredoxin system provides numerous new insights into the mechanism and redox regulation of peroxiredoxins.</p></div><div type="abstract" xml:lang="en"><p><b>GENERAL SIGNIFICANCE</b></p><p>As a member of the special subclass of glutaredoxin/glutathione-dependent peroxiredoxins, the P. falciparum antioxidant protein could become a reference protein for peroxiredoxin catalysis and regulation.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23624334</PMID><DateCompleted><Year>2013</Year><Month>08</Month><Day>19</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1830</Volume><Issue>8</Issue><PubDate><Year>2013</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Plasmodium falciparum antioxidant protein as a model enzyme for a special class of glutaredoxin/glutathione-dependent peroxiredoxins.</ArticleTitle><Pagination><MedlinePgn>4073-90</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbagen.2013.04.020</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0304-4165(13)00148-7</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Peroxiredoxins are important heterogeneous thiol-dependent hydroperoxidases with a variety of isoforms and enzymatic mechanisms. A special subclass of glutaredoxin/glutathione-dependent peroxiredoxins has been discovered in bacteria and eukaryotes during the last decade, but the exact enzymatic mechanisms of these enzymes remain to be unraveled.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">We performed a comprehensive analysis of the enzyme kinetics and redox states of one of these glutaredoxin/glutathione-dependent peroxiredoxins, the antioxidant protein from the malaria parasite Plasmodium falciparum, using steady-state kinetic measurements, site-directed mutagenesis, redox mobility shift assays, gel filtration, and mass spectrometry.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">P. falciparum antioxidant protein requires not only glutaredoxin but also glutathione as a true substrate for the reduction of hydroperoxides. One peroxiredoxin cysteine residue and one glutaredoxin cysteine residue are sufficient for catalysis, however, additional cysteine residues of both proteins result in alternative redox states and conformations in vitro with implications for redox regulation. Our data furthermore point to a glutathione-dependent peroxiredoxin activation and a negative subunit cooperativity.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">The investigated glutaredoxin/glutathione/peroxiredoxin system provides numerous new insights into the mechanism and redox regulation of peroxiredoxins.</AbstractText><AbstractText Label="GENERAL SIGNIFICANCE" NlmCategory="CONCLUSIONS">As a member of the special subclass of glutaredoxin/glutathione-dependent peroxiredoxins, the P. falciparum antioxidant protein could become a reference protein for peroxiredoxin catalysis and regulation.</AbstractText><CopyrightInformation>Copyright © 2013 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Djuika</LastName><ForeName>Carine F</ForeName><Initials>CF</Initials><AffiliationInfo><Affiliation>Department of Parasitology, Ruprecht-Karls University, Heidelberg, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fiedler</LastName><ForeName>Sabine</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Schnölzer</LastName><ForeName>Martina</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Sanchez</LastName><ForeName>Cecilia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Lanzer</LastName><ForeName>Michael</ForeName><Initials>M</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></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>04</Month><Day>24</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta</MedlineTA><NlmUniqueID>0217513</NlmUniqueID><ISSNLinking>0006-3002</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015800">Protozoan Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010963" MajorTopicYN="N">Plasmodium falciparum</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D055503" MajorTopicYN="N">Protein Multimerization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015800" MajorTopicYN="N">Protozoan Proteins</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2013</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2013</Year><Month>04</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2013</Year><Month>04</Month><Day>16</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2013</Year><Month>4</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2013</Year><Month>4</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>8</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23624334</ArticleId><ArticleId IdType="pii">S0304-4165(13)00148-7</ArticleId><ArticleId IdType="doi">10.1016/j.bbagen.2013.04.020</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bade-Wurtemberg</li><li>District de Karlsruhe</li></region><settlement><li>Heidelberg</li></settlement></list><tree><noCountry><name sortKey="Deponte, Marcel" sort="Deponte, Marcel" uniqKey="Deponte M" first="Marcel" last="Deponte">Marcel Deponte</name><name sortKey="Fiedler, Sabine" sort="Fiedler, Sabine" uniqKey="Fiedler S" first="Sabine" last="Fiedler">Sabine Fiedler</name><name sortKey="Lanzer, Michael" sort="Lanzer, Michael" uniqKey="Lanzer M" first="Michael" last="Lanzer">Michael Lanzer</name><name sortKey="Sanchez, Cecilia" sort="Sanchez, Cecilia" uniqKey="Sanchez C" first="Cecilia" last="Sanchez">Cecilia Sanchez</name><name sortKey="Schnolzer, Martina" sort="Schnolzer, Martina" uniqKey="Schnolzer M" first="Martina" last="Schnölzer">Martina Schnölzer</name></noCountry><country name="Allemagne"><region name="Bade-Wurtemberg"><name sortKey="Djuika, Carine F" sort="Djuika, Carine F" uniqKey="Djuika C" first="Carine F" last="Djuika">Carine F. 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