Identification of novel targets of cyanobacterial glutaredoxin.
Identifieur interne : 000C79 ( Main/Exploration ); précédent : 000C78; suivant : 000C80Identification of novel targets of cyanobacterial glutaredoxin.
Auteurs : Min Li [République populaire de Chine] ; Qing Yang ; Lianwen Zhang ; Han Li ; Yunluan Cui ; Qingyu WuSource :
- Archives of biochemistry and biophysics [ 0003-9861 ] ; 2007.
Descripteurs français
- KwdFr :
- Catalase (métabolisme), Chromatographie d'affinité (MeSH), Glutarédoxines (MeSH), Gènes bactériens (MeSH), Mutagenèse dirigée (MeSH), Mutation ponctuelle (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Oxydoréduction (MeSH), Peroxidases (métabolisme), Peroxirédoxines (MeSH), Phénotype (MeSH), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Stress oxydatif (MeSH), Substitution d'acide aminé (MeSH), Synechocystis (enzymologie), Synechocystis (génétique), Synechocystis (métabolisme), Thioredoxin-disulfide reductase (métabolisme).
- MESH :
- enzymologie : Synechocystis.
- génétique : Oxidoreductases, Protéines bactériennes, Protéines recombinantes, Synechocystis.
- métabolisme : Catalase, Oxidoreductases, Peroxidases, Protéines bactériennes, Protéines recombinantes, Synechocystis, Thioredoxin-disulfide reductase.
- Chromatographie d'affinité, Glutarédoxines, Gènes bactériens, Mutagenèse dirigée, Mutation ponctuelle, Oxydoréduction, Peroxirédoxines, Phénotype, Stress oxydatif, Substitution d'acide aminé.
English descriptors
- KwdEn :
- Amino Acid Substitution (MeSH), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Catalase (metabolism), Chromatography, Affinity (MeSH), Genes, Bacterial (MeSH), Glutaredoxins (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Oxidative Stress (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Peroxidases (metabolism), Peroxiredoxins (MeSH), Phenotype (MeSH), Point Mutation (MeSH), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Synechocystis (enzymology), Synechocystis (genetics), Synechocystis (metabolism), Thioredoxin-Disulfide Reductase (metabolism).
- MESH :
- chemical , genetics : Bacterial Proteins, Oxidoreductases, Recombinant Proteins.
- chemical , metabolism : Bacterial Proteins, Catalase, Oxidoreductases, Peroxidases, Recombinant Proteins, Thioredoxin-Disulfide Reductase.
- enzymology : Synechocystis.
- genetics : Synechocystis.
- metabolism : Synechocystis.
- Amino Acid Substitution, Chromatography, Affinity, Genes, Bacterial, Glutaredoxins, Mutagenesis, Site-Directed, Oxidation-Reduction, Oxidative Stress, Peroxiredoxins, Phenotype, Point Mutation.
Abstract
Glutaredoxins (Grxs) are small ubiquitous glutathione-disulfide oxidoreductase that reduce disulfide bonds of target proteins and maintain the redox homoeostasis of cells. Disruption of ssr2061 reduced the viability of cells indicated Grx2061 has a protective role against oxidative stress in Synechocystis sp. PCC 6803. To understand the function of Grx2061 in cyanobacteria and its difference from plant, Grx targets were retained specifically on an affinity media coupled with a mutated monocysteinic Grx and identified by mass spectra. Among 42 identified targets, 26 of them are novel ones compared with those known in higher plants. These proteins are supposed to be involved in 12 cellular processes including oxidative stress response, Calvin cycle, protein synthesis, and etc. Biochemical tests highlighted four of them which showed a Grx-dependent activation of peroxiredoxin and deactivation of catalase. Oxidized Grx2061 could keep redox equilibrium with another probable Grx and be reduced by thioredoxin reductase, indicating that Grx2061 can accept electrons from either glutathione or thioredoxin reductase. Our studies suggest Grx2061 in cyanobacteria plays an important role in redox network and its targets are as extensive as that in other organisms.
DOI: 10.1016/j.abb.2006.12.010
PubMed: 17239812
Affiliations:
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last="Li">Han Li</name></author><author><name sortKey="Cui, Yunluan" sort="Cui, Yunluan" uniqKey="Cui Y" first="Yunluan" last="Cui">Yunluan Cui</name></author><author><name sortKey="Wu, Qingyu" sort="Wu, Qingyu" uniqKey="Wu Q" first="Qingyu" last="Wu">Qingyu Wu</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2007">2007</date><idno type="RBID">pubmed:17239812</idno><idno type="pmid">17239812</idno><idno type="doi">10.1016/j.abb.2006.12.010</idno><idno type="wicri:Area/Main/Corpus">000C83</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C83</idno><idno type="wicri:Area/Main/Curation">000C83</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000C83</idno><idno type="wicri:Area/Main/Exploration">000C83</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification of novel targets of cyanobacterial glutaredoxin.</title><author><name 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(MeSH)</term><term>Point Mutation (MeSH)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Synechocystis (enzymology)</term><term>Synechocystis (genetics)</term><term>Synechocystis (metabolism)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Catalase (métabolisme)</term><term>Chromatographie d'affinité (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Gènes bactériens (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Mutation ponctuelle (MeSH)</term><term>Oxidoreductases (génétique)</term><term>Oxidoreductases (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Peroxidases (métabolisme)</term><term>Peroxirédoxines (MeSH)</term><term>Phénotype (MeSH)</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Substitution d'acide aminé (MeSH)</term><term>Synechocystis (enzymologie)</term><term>Synechocystis (génétique)</term><term>Synechocystis (métabolisme)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Oxidoreductases</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Catalase</term><term>Oxidoreductases</term><term>Peroxidases</term><term>Recombinant Proteins</term><term>Thioredoxin-Disulfide Reductase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases</term><term>Protéines bactériennes</term><term>Protéines recombinantes</term><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Synechocystis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Catalase</term><term>Oxidoreductases</term><term>Peroxidases</term><term>Protéines bactériennes</term><term>Protéines recombinantes</term><term>Synechocystis</term><term>Thioredoxin-disulfide reductase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Chromatography, Affinity</term><term>Genes, Bacterial</term><term>Glutaredoxins</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Oxidative Stress</term><term>Peroxiredoxins</term><term>Phenotype</term><term>Point Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Chromatographie d'affinité</term><term>Glutarédoxines</term><term>Gènes bactériens</term><term>Mutagenèse dirigée</term><term>Mutation ponctuelle</term><term>Oxydoréduction</term><term>Peroxirédoxines</term><term>Phénotype</term><term>Stress oxydatif</term><term>Substitution d'acide aminé</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) are small ubiquitous glutathione-disulfide oxidoreductase that reduce disulfide bonds of target proteins and maintain the redox homoeostasis of cells. Disruption of ssr2061 reduced the viability of cells indicated Grx2061 has a protective role against oxidative stress in Synechocystis sp. PCC 6803. To understand the function of Grx2061 in cyanobacteria and its difference from plant, Grx targets were retained specifically on an affinity media coupled with a mutated monocysteinic Grx and identified by mass spectra. Among 42 identified targets, 26 of them are novel ones compared with those known in higher plants. These proteins are supposed to be involved in 12 cellular processes including oxidative stress response, Calvin cycle, protein synthesis, and etc. Biochemical tests highlighted four of them which showed a Grx-dependent activation of peroxiredoxin and deactivation of catalase. Oxidized Grx2061 could keep redox equilibrium with another probable Grx and be reduced by thioredoxin reductase, indicating that Grx2061 can accept electrons from either glutathione or thioredoxin reductase. Our studies suggest Grx2061 in cyanobacteria plays an important role in redox network and its targets are as extensive as that in other organisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17239812</PMID><DateCompleted><Year>2007</Year><Month>03</Month><Day>26</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0003-9861</ISSN><JournalIssue CitedMedium="Print"><Volume>458</Volume><Issue>2</Issue><PubDate><Year>2007</Year><Month>Feb</Month><Day>15</Day></PubDate></JournalIssue><Title>Archives of biochemistry and biophysics</Title><ISOAbbreviation>Arch Biochem Biophys</ISOAbbreviation></Journal><ArticleTitle>Identification of novel targets of cyanobacterial glutaredoxin.</ArticleTitle><Pagination><MedlinePgn>220-8</MedlinePgn></Pagination><Abstract><AbstractText>Glutaredoxins (Grxs) are small ubiquitous glutathione-disulfide oxidoreductase that reduce disulfide bonds of target proteins and maintain the redox homoeostasis of cells. Disruption of ssr2061 reduced the viability of cells indicated Grx2061 has a protective role against oxidative stress in Synechocystis sp. PCC 6803. To understand the function of Grx2061 in cyanobacteria and its difference from plant, Grx targets were retained specifically on an affinity media coupled with a mutated monocysteinic Grx and identified by mass spectra. Among 42 identified targets, 26 of them are novel ones compared with those known in higher plants. These proteins are supposed to be involved in 12 cellular processes including oxidative stress response, Calvin cycle, protein synthesis, and etc. Biochemical tests highlighted four of them which showed a Grx-dependent activation of peroxiredoxin and deactivation of catalase. Oxidized Grx2061 could keep redox equilibrium with another probable Grx and be reduced by thioredoxin reductase, indicating that Grx2061 can accept electrons from either glutathione or thioredoxin reductase. Our studies suggest Grx2061 in cyanobacteria plays an important role in redox network and its targets are as extensive as that in other organisms.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Min</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biological Sciences and Biotechnology, Tsinghua University, Beijing 100084, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Qing</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Lianwen</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Han</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Cui</LastName><ForeName>Yunluan</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Qingyu</ForeName><Initials>Q</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>2007</Year><Month>01</Month><Day>02</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Arch Biochem Biophys</MedlineTA><NlmUniqueID>0372430</NlmUniqueID><ISSNLinking>0003-9861</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.-</RegistryNumber><NameOfSubstance UI="D010544">Peroxidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.15</RegistryNumber><NameOfSubstance UI="D054464">Peroxiredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.6</RegistryNumber><NameOfSubstance UI="D002374">Catalase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.9</RegistryNumber><NameOfSubstance UI="D013880">Thioredoxin-Disulfide Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002374" MajorTopicYN="N">Catalase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002846" MajorTopicYN="N">Chromatography, Affinity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005798" MajorTopicYN="N">Genes, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010544" MajorTopicYN="N">Peroxidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054464" MajorTopicYN="N">Peroxiredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017354" MajorTopicYN="N">Point Mutation</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="D046939" MajorTopicYN="N">Synechocystis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2006</Year><Month>10</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2006</Year><Month>11</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2006</Year><Month>12</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>1</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>3</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>1</Month><Day>24</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17239812</ArticleId><ArticleId IdType="pii">S0003-9861(06)00498-X</ArticleId><ArticleId IdType="doi">10.1016/j.abb.2006.12.010</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Cui, Yunluan" sort="Cui, Yunluan" uniqKey="Cui Y" first="Yunluan" last="Cui">Yunluan Cui</name><name sortKey="Li, Han" sort="Li, Han" uniqKey="Li H" first="Han" last="Li">Han Li</name><name sortKey="Wu, Qingyu" sort="Wu, Qingyu" uniqKey="Wu Q" first="Qingyu" last="Wu">Qingyu Wu</name><name sortKey="Yang, Qing" sort="Yang, Qing" uniqKey="Yang Q" first="Qing" last="Yang">Qing Yang</name><name sortKey="Zhang, Lianwen" sort="Zhang, Lianwen" uniqKey="Zhang L" first="Lianwen" last="Zhang">Lianwen Zhang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Li, Min" sort="Li, Min" uniqKey="Li M" first="Min" last="Li">Min Li</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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