Overexpression of rice glutaredoxins (OsGrxs) significantly reduces arsenite accumulation by maintaining glutathione pool and modulating aquaporins in yeast.
Identifieur interne : 000435 ( Main/Exploration ); précédent : 000434; suivant : 000436Overexpression of rice glutaredoxins (OsGrxs) significantly reduces arsenite accumulation by maintaining glutathione pool and modulating aquaporins in yeast.
Auteurs : Pankaj Kumar Verma [Inde] ; Shikha Verma [Inde] ; Alok Kumar Meher [Inde] ; Veena Pande [Inde] ; Shekhar Mallick [Inde] ; Amit Kumar Bansiwal [Inde] ; Rudra Deo Tripathi [Inde] ; Om Parkash Dhankher [États-Unis] ; Debasis Chakrabarty [Inde]Source :
- Plant physiology and biochemistry : PPB [ 1873-2690 ] ; 2016.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Aquaporines (métabolisme), Arsenate Reductases (métabolisme), Arsénites (métabolisme), Glutarédoxines (métabolisme), Glutathion (métabolisme), Glutathione reductase (métabolisme), Gènes de plante (MeSH), Mutation (génétique), Oryza (génétique), Oryza (métabolisme), Phénotype (MeSH), Protein-disulfide reductase (glutathione) (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme), Test de complémentation (MeSH), Transport biologique (MeSH).
- MESH :
- génétique : ARN messager, Mutation, Oryza, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- métabolisme : ARN messager, Aquaporines, Arsenate Reductases, Arsénites, Glutarédoxines, Glutathion, Glutathione reductase, Oryza, Protein-disulfide reductase (glutathione), Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- Gènes de plante, Phénotype, Test de complémentation, Transport biologique.
English descriptors
- KwdEn :
- Aquaporins (metabolism), Arsenate Reductases (metabolism), Arsenites (metabolism), Biological Transport (MeSH), Genes, Plant (MeSH), Genetic Complementation Test (MeSH), Glutaredoxins (metabolism), Glutathione (metabolism), Glutathione Reductase (metabolism), Mutation (genetics), Oryza (genetics), Oryza (metabolism), Phenotype (MeSH), Protein Disulfide Reductase (Glutathione) (metabolism), RNA, Messenger (genetics), RNA, Messenger (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism).
- MESH :
- chemical , genetics : RNA, Messenger, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Aquaporins, Arsenate Reductases, Arsenites, Glutaredoxins, Glutathione, Glutathione Reductase, Protein Disulfide Reductase (Glutathione), RNA, Messenger, Saccharomyces cerevisiae Proteins.
- genetics : Mutation, Oryza, Saccharomyces cerevisiae.
- metabolism : Oryza, Saccharomyces cerevisiae.
- Biological Transport, Genes, Plant, Genetic Complementation Test, Phenotype.
Abstract
Arsenic (As) is an acute poison and class I carcinogen, can cause a serious health risk. Staple crops like rice are the primary source of As contamination in human food. Rice grown on As contaminated areas accumulates higher As in their edible parts. Based on our previous transcriptome data, two rice glutaredoxins (OsGrx_C7 and OsGrx_C2.1) were identified that showed up-regulated expression during As stress. Here, we report OsGrx_C7 and OsGrx_C2.1 from rice involved in the regulation of intracellular arsenite (AsIII). To elucidate the mechanism of OsGrx mediated As tolerance, both OsGrxs were cloned and expressed in Escherichia coli (Δars) and Saccharomyces cerevisiae mutant strains (Δycf1, Δacr3). The expression of OsGrxs increased As tolerance in E. coli (Δars) mutant strain (up to 4 mM AsV and up to 0.6 mM AsIII). During AsIII exposure, S. cerevisiae (Δacr3) harboring OsGrx_C7 and OsGrx_C2.1 have lower intracellular AsIII accumulation (up to 30.43% and 24.90%, respectively), compared to vector control. Arsenic accumulation in As-sensitive S. cerevisiae mutant (Δycf1) also reduced significantly on exposure to inorganic As. The expression of OsGrxs in yeast maintained intracellular GSH pool and increased extracellular GSH concentration. Purified OsGrxs displays in vitro GSH-disulfide oxidoreductase, glutathione reductase and arsenate reductase activities. Also, both OsGrxs are involved in AsIII extrusion by altering the Fps1 transcripts in yeast and protect the cell by maintaining cellular GSH pool. Thus, our results strongly suggest that OsGrxs play a crucial role in the maintenance of the intracellular GSH pool and redox status of the cell during both AsV and AsIII stress and might be involved in regulating intracellular AsIII levels by modulation of aquaporin expression and functions.
DOI: 10.1016/j.plaphy.2016.04.052
PubMed: 27174139
Affiliations:
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Department of Biotechnology, Kumaun University, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India; Department of Biotechnology, Kumaun University</wicri:regionArea><wicri:noRegion>Kumaun University</wicri:noRegion></affiliation></author><author><name sortKey="Verma, Shikha" sort="Verma, Shikha" uniqKey="Verma S" first="Shikha" last="Verma">Shikha Verma</name><affiliation wicri:level="1"><nlm:affiliation>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India; Department of Biotechnology, Kumaun University, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India; Department of Biotechnology, Kumaun University</wicri:regionArea><wicri:noRegion>Kumaun University</wicri:noRegion></affiliation></author><author><name sortKey="Meher, Alok Kumar" sort="Meher, Alok Kumar" uniqKey="Meher A" first="Alok Kumar" last="Meher">Alok Kumar Meher</name><affiliation wicri:level="1"><nlm:affiliation>Environmental Material Division, CSIR-National Environmental Engineering Research Institute, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Environmental Material Division, CSIR-National Environmental Engineering Research Institute</wicri:regionArea><wicri:noRegion>CSIR-National Environmental Engineering Research Institute</wicri:noRegion></affiliation></author><author><name sortKey="Pande, Veena" sort="Pande, Veena" uniqKey="Pande V" first="Veena" last="Pande">Veena Pande</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biotechnology, Kumaun University, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Department of Biotechnology, Kumaun University</wicri:regionArea><wicri:noRegion>Kumaun University</wicri:noRegion></affiliation></author><author><name sortKey="Mallick, Shekhar" sort="Mallick, Shekhar" uniqKey="Mallick S" first="Shekhar" last="Mallick">Shekhar Mallick</name><affiliation wicri:level="1"><nlm:affiliation>Environmental Biotechnology Division, CSIR-National Botanical Research Institute, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Environmental Biotechnology Division, CSIR-National Botanical Research Institute</wicri:regionArea><wicri:noRegion>CSIR-National Botanical Research Institute</wicri:noRegion></affiliation></author><author><name sortKey="Bansiwal, Amit Kumar" sort="Bansiwal, Amit Kumar" uniqKey="Bansiwal A" first="Amit Kumar" last="Bansiwal">Amit Kumar Bansiwal</name><affiliation wicri:level="1"><nlm:affiliation>Environmental Material Division, CSIR-National Environmental Engineering Research Institute, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Environmental Material Division, CSIR-National Environmental Engineering Research Institute</wicri:regionArea><wicri:noRegion>CSIR-National Environmental Engineering Research Institute</wicri:noRegion></affiliation></author><author><name sortKey="Tripathi, Rudra Deo" sort="Tripathi, Rudra Deo" uniqKey="Tripathi R" first="Rudra Deo" last="Tripathi">Rudra Deo Tripathi</name><affiliation wicri:level="1"><nlm:affiliation>Environmental Biotechnology Division, CSIR-National Botanical Research Institute, India.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Environmental Biotechnology Division, CSIR-National Botanical Research Institute</wicri:regionArea><wicri:noRegion>CSIR-National Botanical Research Institute</wicri:noRegion></affiliation></author><author><name sortKey="Dhankher, Om Parkash" sort="Dhankher, Om Parkash" uniqKey="Dhankher O" first="Om Parkash" last="Dhankher">Om Parkash Dhankher</name><affiliation wicri:level="4"><nlm:affiliation>Stockbridge School of Agriculture, University of Massachusetts, Amherst, MA, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Stockbridge School of Agriculture, University of Massachusetts, Amherst, MA</wicri:regionArea><placeName><region type="state">Massachusetts</region><settlement type="city">Amherst (Massachusetts)</settlement></placeName><orgName type="university">Université du Massachusetts</orgName></affiliation></author><author><name sortKey="Chakrabarty, Debasis" sort="Chakrabarty, Debasis" uniqKey="Chakrabarty D" first="Debasis" last="Chakrabarty">Debasis Chakrabarty</name><affiliation wicri:level="1"><nlm:affiliation>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India. Electronic address: chakrabartyd@nbri.res.in.</nlm:affiliation><country xml:lang="fr">Inde</country><wicri:regionArea>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute</wicri:regionArea><wicri:noRegion>CSIR-National Botanical Research Institute</wicri:noRegion></affiliation></author></analytic><series><title level="j">Plant physiology and biochemistry : PPB</title><idno type="eISSN">1873-2690</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aquaporins (metabolism)</term><term>Arsenate Reductases (metabolism)</term><term>Arsenites (metabolism)</term><term>Biological Transport (MeSH)</term><term>Genes, Plant (MeSH)</term><term>Genetic Complementation Test (MeSH)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Glutathione Reductase (metabolism)</term><term>Mutation (genetics)</term><term>Oryza (genetics)</term><term>Oryza (metabolism)</term><term>Phenotype (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (metabolism)</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term><term>ARN messager (métabolisme)</term><term>Aquaporines (métabolisme)</term><term>Arsenate Reductases (métabolisme)</term><term>Arsénites (métabolisme)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Glutathione reductase (métabolisme)</term><term>Gènes de plante (MeSH)</term><term>Mutation (génétique)</term><term>Oryza (génétique)</term><term>Oryza (métabolisme)</term><term>Phénotype (MeSH)</term><term>Protein-disulfide reductase (glutathione) (métabolisme)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Test de complémentation (MeSH)</term><term>Transport biologique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>RNA, Messenger</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aquaporins</term><term>Arsenate Reductases</term><term>Arsenites</term><term>Glutaredoxins</term><term>Glutathione</term><term>Glutathione Reductase</term><term>Protein Disulfide Reductase (Glutathione)</term><term>RNA, Messenger</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mutation</term><term>Oryza</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN messager</term><term>Mutation</term><term>Oryza</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Oryza</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Aquaporines</term><term>Arsenate Reductases</term><term>Arsénites</term><term>Glutarédoxines</term><term>Glutathion</term><term>Glutathione reductase</term><term>Oryza</term><term>Protein-disulfide reductase (glutathione)</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biological Transport</term><term>Genes, Plant</term><term>Genetic Complementation Test</term><term>Phenotype</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Gènes de plante</term><term>Phénotype</term><term>Test de complémentation</term><term>Transport biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Arsenic (As) is an acute poison and class I carcinogen, can cause a serious health risk. Staple crops like rice are the primary source of As contamination in human food. Rice grown on As contaminated areas accumulates higher As in their edible parts. Based on our previous transcriptome data, two rice glutaredoxins (OsGrx_C7 and OsGrx_C2.1) were identified that showed up-regulated expression during As stress. Here, we report OsGrx_C7 and OsGrx_C2.1 from rice involved in the regulation of intracellular arsenite (AsIII). To elucidate the mechanism of OsGrx mediated As tolerance, both OsGrxs were cloned and expressed in Escherichia coli (Δars) and Saccharomyces cerevisiae mutant strains (Δycf1, Δacr3). The expression of OsGrxs increased As tolerance in E. coli (Δars) mutant strain (up to 4 mM AsV and up to 0.6 mM AsIII). During AsIII exposure, S. cerevisiae (Δacr3) harboring OsGrx_C7 and OsGrx_C2.1 have lower intracellular AsIII accumulation (up to 30.43% and 24.90%, respectively), compared to vector control. Arsenic accumulation in As-sensitive S. cerevisiae mutant (Δycf1) also reduced significantly on exposure to inorganic As. The expression of OsGrxs in yeast maintained intracellular GSH pool and increased extracellular GSH concentration. Purified OsGrxs displays in vitro GSH-disulfide oxidoreductase, glutathione reductase and arsenate reductase activities. Also, both OsGrxs are involved in AsIII extrusion by altering the Fps1 transcripts in yeast and protect the cell by maintaining cellular GSH pool. Thus, our results strongly suggest that OsGrxs play a crucial role in the maintenance of the intracellular GSH pool and redox status of the cell during both AsV and AsIII stress and might be involved in regulating intracellular AsIII levels by modulation of aquaporin expression and functions. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27174139</PMID><DateCompleted><Year>2017</Year><Month>03</Month><Day>27</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1873-2690</ISSN><JournalIssue CitedMedium="Internet"><Volume>106</Volume><PubDate><Year>2016</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Plant physiology and biochemistry : PPB</Title><ISOAbbreviation>Plant Physiol Biochem</ISOAbbreviation></Journal><ArticleTitle>Overexpression of rice glutaredoxins (OsGrxs) significantly reduces arsenite accumulation by maintaining glutathione pool and modulating aquaporins in yeast.</ArticleTitle><Pagination><MedlinePgn>208-17</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.plaphy.2016.04.052</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0981-9428(16)30167-X</ELocationID><Abstract><AbstractText>Arsenic (As) is an acute poison and class I carcinogen, can cause a serious health risk. Staple crops like rice are the primary source of As contamination in human food. Rice grown on As contaminated areas accumulates higher As in their edible parts. Based on our previous transcriptome data, two rice glutaredoxins (OsGrx_C7 and OsGrx_C2.1) were identified that showed up-regulated expression during As stress. Here, we report OsGrx_C7 and OsGrx_C2.1 from rice involved in the regulation of intracellular arsenite (AsIII). To elucidate the mechanism of OsGrx mediated As tolerance, both OsGrxs were cloned and expressed in Escherichia coli (Δars) and Saccharomyces cerevisiae mutant strains (Δycf1, Δacr3). The expression of OsGrxs increased As tolerance in E. coli (Δars) mutant strain (up to 4 mM AsV and up to 0.6 mM AsIII). During AsIII exposure, S. cerevisiae (Δacr3) harboring OsGrx_C7 and OsGrx_C2.1 have lower intracellular AsIII accumulation (up to 30.43% and 24.90%, respectively), compared to vector control. Arsenic accumulation in As-sensitive S. cerevisiae mutant (Δycf1) also reduced significantly on exposure to inorganic As. The expression of OsGrxs in yeast maintained intracellular GSH pool and increased extracellular GSH concentration. Purified OsGrxs displays in vitro GSH-disulfide oxidoreductase, glutathione reductase and arsenate reductase activities. Also, both OsGrxs are involved in AsIII extrusion by altering the Fps1 transcripts in yeast and protect the cell by maintaining cellular GSH pool. Thus, our results strongly suggest that OsGrxs play a crucial role in the maintenance of the intracellular GSH pool and redox status of the cell during both AsV and AsIII stress and might be involved in regulating intracellular AsIII levels by modulation of aquaporin expression and functions. </AbstractText><CopyrightInformation>Copyright © 2016 Elsevier Masson SAS. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Verma</LastName><ForeName>Pankaj Kumar</ForeName><Initials>PK</Initials><AffiliationInfo><Affiliation>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India; Department of Biotechnology, Kumaun University, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Verma</LastName><ForeName>Shikha</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India; Department of Biotechnology, Kumaun University, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Meher</LastName><ForeName>Alok Kumar</ForeName><Initials>AK</Initials><AffiliationInfo><Affiliation>Environmental Material Division, CSIR-National Environmental Engineering Research Institute, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pande</LastName><ForeName>Veena</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Biotechnology, Kumaun University, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mallick</LastName><ForeName>Shekhar</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Environmental Biotechnology Division, CSIR-National Botanical Research Institute, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bansiwal</LastName><ForeName>Amit Kumar</ForeName><Initials>AK</Initials><AffiliationInfo><Affiliation>Environmental Material Division, CSIR-National Environmental Engineering Research Institute, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tripathi</LastName><ForeName>Rudra Deo</ForeName><Initials>RD</Initials><AffiliationInfo><Affiliation>Environmental Biotechnology Division, CSIR-National Botanical Research Institute, India.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dhankher</LastName><ForeName>Om Parkash</ForeName><Initials>OP</Initials><AffiliationInfo><Affiliation>Stockbridge School of Agriculture, University of Massachusetts, Amherst, MA, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chakrabarty</LastName><ForeName>Debasis</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Genetics and Molecular Biology Division, CSIR-National Botanical Research Institute, India. Electronic address: chakrabartyd@nbri.res.in.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>04</Month><Day>30</Day></ArticleDate></Article><MedlineJournalInfo><Country>France</Country><MedlineTA>Plant Physiol Biochem</MedlineTA><NlmUniqueID>9882449</NlmUniqueID><ISSNLinking>0981-9428</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020346">Aquaporins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018053">Arsenites</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D012333">RNA, Messenger</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.20.-</RegistryNumber><NameOfSubstance UI="D053502">Arsenate Reductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.1.7</RegistryNumber><NameOfSubstance UI="D005980">Glutathione Reductase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>N5509X556J</RegistryNumber><NameOfSubstance UI="C015001">arsenite</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D020346" MajorTopicYN="N">Aquaporins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053502" MajorTopicYN="N">Arsenate Reductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018053" MajorTopicYN="N">Arsenites</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001692" MajorTopicYN="N">Biological Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005816" MajorTopicYN="N">Genetic Complementation Test</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005980" MajorTopicYN="N">Glutathione Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="N">Protein Disulfide Reductase (Glutathione)</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012333" MajorTopicYN="N">RNA, Messenger</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029701" MajorTopicYN="N">Saccharomyces cerevisiae Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Arsenic</Keyword><Keyword MajorTopicYN="N">GSH</Keyword><Keyword MajorTopicYN="N">Glutaredoxin</Keyword><Keyword MajorTopicYN="N">Oryza sativa</Keyword><Keyword MajorTopicYN="N">OsGrxs</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>03</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2016</Year><Month>04</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>04</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>5</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>5</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>3</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27174139</ArticleId><ArticleId IdType="pii">S0981-9428(16)30167-X</ArticleId><ArticleId IdType="doi">10.1016/j.plaphy.2016.04.052</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Inde</li><li>États-Unis</li></country><region><li>Massachusetts</li></region><settlement><li>Amherst (Massachusetts)</li></settlement><orgName><li>Université du Massachusetts</li></orgName></list><tree><country name="Inde"><noRegion><name sortKey="Verma, Pankaj Kumar" sort="Verma, Pankaj Kumar" uniqKey="Verma P" first="Pankaj Kumar" last="Verma">Pankaj Kumar Verma</name></noRegion><name sortKey="Bansiwal, Amit Kumar" sort="Bansiwal, Amit Kumar" uniqKey="Bansiwal A" first="Amit Kumar" last="Bansiwal">Amit Kumar Bansiwal</name><name sortKey="Chakrabarty, Debasis" sort="Chakrabarty, Debasis" uniqKey="Chakrabarty D" first="Debasis" last="Chakrabarty">Debasis Chakrabarty</name><name sortKey="Mallick, Shekhar" sort="Mallick, Shekhar" uniqKey="Mallick S" first="Shekhar" last="Mallick">Shekhar Mallick</name><name sortKey="Meher, Alok Kumar" sort="Meher, Alok Kumar" uniqKey="Meher A" first="Alok Kumar" last="Meher">Alok Kumar Meher</name><name sortKey="Pande, Veena" sort="Pande, Veena" uniqKey="Pande V" first="Veena" last="Pande">Veena Pande</name><name sortKey="Tripathi, Rudra Deo" sort="Tripathi, Rudra Deo" uniqKey="Tripathi R" first="Rudra Deo" last="Tripathi">Rudra Deo Tripathi</name><name sortKey="Verma, Shikha" sort="Verma, Shikha" uniqKey="Verma S" first="Shikha" last="Verma">Shikha Verma</name></country><country name="États-Unis"><region name="Massachusetts"><name sortKey="Dhankher, Om Parkash" sort="Dhankher, Om Parkash" uniqKey="Dhankher O" first="Om Parkash" last="Dhankher">Om Parkash Dhankher</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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