The Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.
Identifieur interne : 000707 ( Main/Exploration ); précédent : 000706; suivant : 000708The Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.
Auteurs : Benoit Marteyn [France] ; Samer Sakr ; Sandrine Farci ; Mariette Bedhomme ; Solenne Chardonnet ; Paulette Decottignies ; Stéphane D. Lemaire ; Corinne Cassier-Chauvat ; Franck ChauvatSource :
- Journal of bacteriology [ 1098-5530 ] ; 2013.
Descripteurs français
- KwdFr :
- Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Mercure (métabolisme), Mercure (toxicité), Motifs et domaines d'intéraction protéique (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Régulation de l'expression des gènes bactériens (MeSH), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Synechocystis (croissance et développement), Synechocystis (effets des médicaments et des substances chimiques), Synechocystis (enzymologie), Synechocystis (génétique), Techniques de double hybride (MeSH), Uranium (métabolisme), Uranium (toxicité).
- MESH :
- composition chimique : Glutarédoxines, Oxidoreductases.
- croissance et développement : Synechocystis.
- effets des médicaments et des substances chimiques : Synechocystis.
- enzymologie : Synechocystis.
- génétique : Glutarédoxines, Oxidoreductases, Synechocystis.
- métabolisme : Glutarédoxines, Mercure, Oxidoreductases, Uranium.
- toxicité : Mercure, Uranium.
- Motifs et domaines d'intéraction protéique, Oxydoréduction, Régulation de l'expression des gènes bactériens, Régulation de l'expression des gènes codant pour des enzymes, Techniques de double hybride.
English descriptors
- KwdEn :
- Gene Expression Regulation, Bacterial (MeSH), Gene Expression Regulation, Enzymologic (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Mercury (metabolism), Mercury (toxicity), Oxidation-Reduction (MeSH), Oxidoreductases (chemistry), Oxidoreductases (genetics), Oxidoreductases (metabolism), Protein Interaction Domains and Motifs (MeSH), Synechocystis (drug effects), Synechocystis (enzymology), Synechocystis (genetics), Synechocystis (growth & development), Two-Hybrid System Techniques (MeSH), Uranium (metabolism), Uranium (toxicity).
- MESH :
- chemical , chemistry : Glutaredoxins, Oxidoreductases.
- chemical , genetics : Glutaredoxins, Oxidoreductases.
- chemical , metabolism : Glutaredoxins, Mercury, Oxidoreductases, Uranium.
- chemical , toxicity : Mercury, Uranium.
- drug effects : Synechocystis.
- enzymology : Synechocystis.
- genetics : Synechocystis.
- growth & development : Synechocystis.
- Gene Expression Regulation, Bacterial, Gene Expression Regulation, Enzymologic, Oxidation-Reduction, Protein Interaction Domains and Motifs, Two-Hybrid System Techniques.
Abstract
In a continuing effort to analyze the selectivity/redundancy of the three glutaredoxin (Grx) enzymes of the model cyanobacterium Synechocystis PCC6803, we have characterized an enzyme system that plays a crucial role in protection against two toxic metal pollutants, mercury and uranium. The present data show that Grx1 (Slr1562 in CyanoBase) selectively interacts with the presumptive mercuric reductase protein (Slr1849). This MerA enzyme plays a crucial role in cell defense against both mercuric and uranyl ions, in catalyzing their NADPH-driven reduction. Like MerA, Grx1 operates in cell protection against both mercury and uranium. The Grx1-MerA interaction requires cysteine 86 (C86) of Grx1 and C78 of MerA, which is critical for its reductase activity. MerA can be inhibited by glutathionylation and subsequently reactivated by Grx1, likely through deglutathionylation. The two Grx1 residues C31, which belongs to the redox active site (CX(2)C), and C86, which operates in MerA interactions, are both required for reactivation of MerA. These novel findings emphasize the role of glutaredoxins in tolerance to metal stress as well as the evolutionary conservation of the glutathionylation process, so far described mostly for eukaryotes.
DOI: 10.1128/JB.00272-13
PubMed: 23852862
PubMed Central: PMC3754753
Affiliations:
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(chemistry)</term><term>Oxidoreductases (genetics)</term><term>Oxidoreductases (metabolism)</term><term>Protein Interaction Domains and Motifs (MeSH)</term><term>Synechocystis (drug effects)</term><term>Synechocystis (enzymology)</term><term>Synechocystis (genetics)</term><term>Synechocystis (growth & development)</term><term>Two-Hybrid System Techniques (MeSH)</term><term>Uranium (metabolism)</term><term>Uranium (toxicity)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Mercure (métabolisme)</term><term>Mercure (toxicité)</term><term>Motifs et domaines d'intéraction protéique (MeSH)</term><term>Oxidoreductases (composition chimique)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Régulation de l'expression des gènes bactériens (MeSH)</term><term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term><term>Synechocystis (croissance et développement)</term><term>Synechocystis (effets des médicaments et des substances chimiques)</term><term>Synechocystis (enzymologie)</term><term>Synechocystis (génétique)</term><term>Techniques de double hybride (MeSH)</term><term>Uranium (métabolisme)</term><term>Uranium (toxicité)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Mercury</term><term>Oxidoreductases</term><term>Uranium</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Mercury</term><term>Uranium</term></keywords><keywords 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hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In a continuing effort to analyze the selectivity/redundancy of the three glutaredoxin (Grx) enzymes of the model cyanobacterium Synechocystis PCC6803, we have characterized an enzyme system that plays a crucial role in protection against two toxic metal pollutants, mercury and uranium. The present data show that Grx1 (Slr1562 in CyanoBase) selectively interacts with the presumptive mercuric reductase protein (Slr1849). This MerA enzyme plays a crucial role in cell defense against both mercuric and uranyl ions, in catalyzing their NADPH-driven reduction. Like MerA, Grx1 operates in cell protection against both mercury and uranium. The Grx1-MerA interaction requires cysteine 86 (C86) of Grx1 and C78 of MerA, which is critical for its reductase activity. MerA can be inhibited by glutathionylation and subsequently reactivated by Grx1, likely through deglutathionylation. The two Grx1 residues C31, which belongs to the redox active site (CX(2)C), and C86, which operates in MerA interactions, are both required for reactivation of MerA. These novel findings emphasize the role of glutaredoxins in tolerance to metal stress as well as the evolutionary conservation of the glutathionylation process, so far described mostly for eukaryotes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23852862</PMID><DateCompleted><Year>2013</Year><Month>11</Month><Day>05</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5530</ISSN><JournalIssue CitedMedium="Internet"><Volume>195</Volume><Issue>18</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Journal of bacteriology</Title><ISOAbbreviation>J Bacteriol</ISOAbbreviation></Journal><ArticleTitle>The Synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme.</ArticleTitle><Pagination><MedlinePgn>4138-45</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JB.00272-13</ELocationID><Abstract><AbstractText>In a continuing effort to analyze the selectivity/redundancy of the three glutaredoxin (Grx) enzymes of the model cyanobacterium Synechocystis PCC6803, we have characterized an enzyme system that plays a crucial role in protection against two toxic metal pollutants, mercury and uranium. The present data show that Grx1 (Slr1562 in CyanoBase) selectively interacts with the presumptive mercuric reductase protein (Slr1849). This MerA enzyme plays a crucial role in cell defense against both mercuric and uranyl ions, in catalyzing their NADPH-driven reduction. Like MerA, Grx1 operates in cell protection against both mercury and uranium. The Grx1-MerA interaction requires cysteine 86 (C86) of Grx1 and C78 of MerA, which is critical for its reductase activity. MerA can be inhibited by glutathionylation and subsequently reactivated by Grx1, likely through deglutathionylation. The two Grx1 residues C31, which belongs to the redox active site (CX(2)C), and C86, which operates in MerA interactions, are both required for reactivation of MerA. These novel findings emphasize the role of glutaredoxins in tolerance to metal stress as well as the evolutionary conservation of the glutathionylation process, so far described mostly for eukaryotes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Marteyn</LastName><ForeName>Benoit</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>UMR8221, CEA, CNRS, Université Paris Sud, iBiTec-S, LBBC, Gif sur Yvette, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sakr</LastName><ForeName>Samer</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Farci</LastName><ForeName>Sandrine</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Bedhomme</LastName><ForeName>Mariette</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Chardonnet</LastName><ForeName>Solenne</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Decottignies</LastName><ForeName>Paulette</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Lemaire</LastName><ForeName>Stéphane D</ForeName><Initials>SD</Initials></Author><Author ValidYN="Y"><LastName>Cassier-Chauvat</LastName><ForeName>Corinne</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Chauvat</LastName><ForeName>Franck</ForeName><Initials>F</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>2013</Year><Month>07</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Bacteriol</MedlineTA><NlmUniqueID>2985120R</NlmUniqueID><ISSNLinking>0021-9193</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>4OC371KSTK</RegistryNumber><NameOfSubstance UI="D014501">Uranium</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.16.-</RegistryNumber><NameOfSubstance UI="C021551">mercuric reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>FXS1BY2PGL</RegistryNumber><NameOfSubstance UI="D008628">Mercury</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D015964" MajorTopicYN="Y">Gene Expression Regulation, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015971" MajorTopicYN="Y">Gene Expression Regulation, Enzymologic</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008628" MajorTopicYN="N">Mercury</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000633" MajorTopicYN="N">toxicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046939" MajorTopicYN="N">Synechocystis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014501" MajorTopicYN="N">Uranium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000633" 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Paris-Sud</li></orgName></list><tree><noCountry><name sortKey="Bedhomme, Mariette" sort="Bedhomme, Mariette" uniqKey="Bedhomme M" first="Mariette" last="Bedhomme">Mariette Bedhomme</name><name sortKey="Cassier Chauvat, Corinne" sort="Cassier Chauvat, Corinne" uniqKey="Cassier Chauvat C" first="Corinne" last="Cassier-Chauvat">Corinne Cassier-Chauvat</name><name sortKey="Chardonnet, Solenne" sort="Chardonnet, Solenne" uniqKey="Chardonnet S" first="Solenne" last="Chardonnet">Solenne Chardonnet</name><name sortKey="Chauvat, Franck" sort="Chauvat, Franck" uniqKey="Chauvat F" first="Franck" last="Chauvat">Franck Chauvat</name><name sortKey="Decottignies, Paulette" sort="Decottignies, Paulette" uniqKey="Decottignies P" first="Paulette" last="Decottignies">Paulette Decottignies</name><name sortKey="Farci, Sandrine" sort="Farci, Sandrine" uniqKey="Farci S" first="Sandrine" last="Farci">Sandrine Farci</name><name sortKey="Lemaire, Stephane D" sort="Lemaire, Stephane D" uniqKey="Lemaire S" first="Stéphane D" last="Lemaire">Stéphane D. Lemaire</name><name sortKey="Sakr, Samer" sort="Sakr, Samer" uniqKey="Sakr S" first="Samer" last="Sakr">Samer Sakr</name></noCountry><country name="France"><region name="Île-de-France"><name sortKey="Marteyn, Benoit" sort="Marteyn, Benoit" uniqKey="Marteyn B" first="Benoit" last="Marteyn">Benoit Marteyn</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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