PoplarV1, Main, Exploration, bibRecord, 000904

Identification and Characterization of an OSH1 Thiol Reductase from Populus Trichocarpa.

Identifieur interne : 000904 ( Main/Exploration ); précédent : 000903; suivant : 000905

Identification and Characterization of an OSH1 Thiol Reductase from Populus Trichocarpa.

Auteurs : Hui Wei [République populaire de Chine] ; Jie Zhou [République populaire de Chine] ; Chen Xu [République populaire de Chine] ; Ali Movahedi [République populaire de Chine] ; Weibo Sun [République populaire de Chine] ; Dawei Li [République populaire de Chine] ; Qiang Zhuge [République populaire de Chine]

Source :

Cells [ 2073-4409 ] ; 2019.

RBID : pubmed:31892265

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Gene Expression (MeSH), Humans (MeSH), Open Reading Frames (MeSH), Oxidoreductases Acting on Sulfur Group Donors (chemistry), Oxidoreductases Acting on Sulfur Group Donors (genetics), Oxidoreductases Acting on Sulfur Group Donors (isolation & purification), Oxidoreductases Acting on Sulfur Group Donors (metabolism), Phenotype (MeSH), Plants, Genetically Modified (MeSH), Populus (classification), Populus (enzymology), Populus (genetics), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Recombinant Proteins (metabolism), Stress, Physiological (MeSH), Transcription, Genetic (MeSH).
MESH :
- chemical , chemistry : Oxidoreductases Acting on Sulfur Group Donors, Recombinant Proteins.
- chemical , genetics : Oxidoreductases Acting on Sulfur Group Donors, Recombinant Proteins.
- chemical , isolation & purification : Oxidoreductases Acting on Sulfur Group Donors, Recombinant Proteins.
- chemical , metabolism : Oxidoreductases Acting on Sulfur Group Donors, Recombinant Proteins.
- classification : Populus.
- enzymology : Populus.
- genetics : Populus.
- Amino Acid Sequence, Gene Expression, Humans, Open Reading Frames, Phenotype, Plants, Genetically Modified, Stress, Physiological, Transcription, Genetic.

Abstract

Interferon gamma-induced lysosomal thiol reductase (GILT) is abundantly expressed in antigen-presenting cells and participates in the treatment and presentation of antigens by major histocompatibility complex II. Also, GILT catalyzes the reduction of disulfide bonds, which plays an important role in cellular immunity. (1) Background: At present, the studies of GILT have mainly focused on animals. In plants, GILT homologous gene (Arabidopsis thalianaOSH1: AtOSH1) was discovered in the forward screen of mutants with compromised responses to sulphur nutrition. However, the complete properties and functions of poplar OSH1 are unclear. In addition, CdCl₂ stress is swiftly engulfing the limited land resources on which humans depend, restricting agricultural production. (2) Methods: A prokaryotic expression system was used to produce recombinant PtOSH1 protein, and Western blotting was performed to identify its activity. In addition, a simplified version of the floral-dip method was used to transform A. thaliana. (3) Results: Here, we describe the identification and characterization of OSH1 from Populus trichocarpa. The deduced PtOSH1 sequence contained CQHGX2ECX2NX4C and CXXC motifs. The transcript level of PtOSH1 was increased by cadmium (Cd) treatment. In addition, recombinant PtOSH1 reduced disulfide bonds. A stress assay showed that PtOSH1-overexpressing (OE) A. thaliana lines had greater resistance to Cd than wild-type (WT) plants. Also, the activities of superoxide dismutase (SOD), peroxidase (POD), and catalase (CAT) in PtOSH1-OE plants were significantly higher than those in WT A. thaliana. These results indicate that PtOSH1 likely plays an important role in the response to Cd by regulating the reactive oxygen species (ROS)-scavenging system. (4) Conclusions: PtOSH1 catalyzes the reduction of disulfide bonds and behaves as a sulfhydryl reductase under acidic conditions. The overexpression of PtOSH1 in A. thaliana promoted root development, fresh weight, and dry weight; upregulated the expression levels of ROS scavenging-related genes; and improved the activity of antioxidant enzymes, enhancing plant tolerance to cadmium (Cd) stress. This study aimed to provide guidance that will facilitate future studies of the function of PtOSH1 in the response of plants to Cd stress.

DOI: 10.3390/cells9010076
PubMed: 31892265
PubMed Central: PMC7017176

Affiliations:

République populaire de Chine

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000538
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Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en">Identification and Characterization of an OSH1 Thiol Reductase from <i>Populus Trichocarpa</i>
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<affiliation wicri:level="1"><nlm:affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
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<author><name sortKey="Zhou, Jie" sort="Zhou, Jie" uniqKey="Zhou J" first="Jie" last="Zhou">Jie Zhou</name>
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<author><name sortKey="Xu, Chen" sort="Xu, Chen" uniqKey="Xu C" first="Chen" last="Xu">Chen Xu</name>
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<country xml:lang="fr">République populaire de Chine</country>
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<wicri:regionArea>Jiangsu Provincial Key Construction Laboratory of Special Biomass Resource Utilization, Nanjing Key Laboratory of Quality and Safety of Agricultural Products, Nanjing Xiaozhuang University, Nanjing 211171</wicri:regionArea>
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</affiliation>
</author>
<author><name sortKey="Movahedi, Ali" sort="Movahedi, Ali" uniqKey="Movahedi A" first="Ali" last="Movahedi">Ali Movahedi</name>
<affiliation wicri:level="1"><nlm:affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</nlm:affiliation>
<country xml:lang="fr">République populaire de Chine</country>
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</affiliation>
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<author><name sortKey="Sun, Weibo" sort="Sun, Weibo" uniqKey="Sun W" first="Weibo" last="Sun">Weibo Sun</name>
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</affiliation>
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<author><name sortKey="Zhuge, Qiang" sort="Zhuge, Qiang" uniqKey="Zhuge Q" first="Qiang" last="Zhuge">Qiang Zhuge</name>
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<series><title level="j">Cells</title>
<idno type="eISSN">2073-4409</idno>
<imprint><date when="2019" type="published">2019</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Gene Expression (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Open Reading Frames (MeSH)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (chemistry)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (genetics)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (isolation & purification)</term>
<term>Oxidoreductases Acting on Sulfur Group Donors (metabolism)</term>
<term>Phenotype (MeSH)</term>
<term>Plants, Genetically Modified (MeSH)</term>
<term>Populus (classification)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (genetics)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Recombinant Proteins (metabolism)</term>
<term>Stress, Physiological (MeSH)</term>
<term>Transcription, Genetic (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cadres ouverts de lecture (MeSH)</term>
<term>Expression des gènes (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Oxidoreductases acting on sulfur group donors (composition chimique)</term>
<term>Oxidoreductases acting on sulfur group donors (génétique)</term>
<term>Oxidoreductases acting on sulfur group donors (isolement et purification)</term>
<term>Oxidoreductases acting on sulfur group donors (métabolisme)</term>
<term>Phénotype (MeSH)</term>
<term>Populus (classification)</term>
<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (génétique)</term>
<term>Protéines recombinantes (isolement et purification)</term>
<term>Protéines recombinantes (métabolisme)</term>
<term>Stress physiologique (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Transcription génétique (MeSH)</term>
<term>Végétaux génétiquement modifiés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases Acting on Sulfur Group Donors</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="classification" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases acting on sulfur group donors</term>
<term>Populus</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Oxidoreductases acting on sulfur group donors</term>
<term>Populus</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Oxidoreductases acting on sulfur group donors</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Oxidoreductases acting on sulfur group donors</term>
<term>Protéines recombinantes</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Gene Expression</term>
<term>Humans</term>
<term>Open Reading Frames</term>
<term>Phenotype</term>
<term>Plants, Genetically Modified</term>
<term>Stress, Physiological</term>
<term>Transcription, Genetic</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cadres ouverts de lecture</term>
<term>Expression des gènes</term>
<term>Humains</term>
<term>Phénotype</term>
<term>Stress physiologique</term>
<term>Séquence d'acides aminés</term>
<term>Transcription génétique</term>
<term>Végétaux génétiquement modifiés</term>
</keywords>
</textClass>
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<front><div type="abstract" xml:lang="en">Interferon gamma-induced lysosomal thiol reductase (GILT) is abundantly expressed in antigen-presenting cells and participates in the treatment and presentation of antigens by major histocompatibility complex II. Also, GILT catalyzes the reduction of disulfide bonds, which plays an important role in cellular immunity. (1) Background: At present, the studies of GILT have mainly focused on animals. In plants, GILT homologous gene (<i>Arabidopsis thaliana</i>
<i>OSH1</i>
: <i>AtOSH1</i>
) was discovered in the forward screen of mutants with compromised responses to sulphur nutrition. However, the complete properties and functions of poplar OSH1 are unclear. In addition, CdCl<sub>2</sub>
 stress is swiftly engulfing the limited land resources on which humans depend, restricting agricultural production. (2) Methods: A prokaryotic expression system was used to produce recombinant PtOSH1 protein, and Western blotting was performed to identify its activity. In addition, a simplified version of the floral-dip method was used to transform <i>A. thaliana</i>
. (3) Results: Here, we describe the identification and characterization of OSH1 from <i>Populus trichocarpa</i>
. The deduced PtOSH1 sequence contained CQHGX2ECX2NX4C and CXXC motifs. The transcript level of <i>PtOSH1</i>
 was increased by cadmium (Cd) treatment. In addition, recombinant PtOSH1 reduced disulfide bonds. A stress assay showed that <i>PtOSH1</i>
-overexpressing (OE) <i>A. thaliana</i>
 lines had greater resistance to Cd than wild-type (WT) plants. Also, the activities of superoxide dismutase (SOD), peroxidase (POD), and catalase (CAT) in <i>PtOSH1</i>
-OE plants were significantly higher than those in WT <i>A. thaliana</i>
. These results indicate that PtOSH1 likely plays an important role in the response to Cd by regulating the reactive oxygen species (ROS)-scavenging system. (4) Conclusions: PtOSH1 catalyzes the reduction of disulfide bonds and behaves as a sulfhydryl reductase under acidic conditions. The overexpression of <i>PtOSH1</i>
 in <i>A. thaliana</i>
 promoted root development, fresh weight, and dry weight; upregulated the expression levels of ROS scavenging-related genes; and improved the activity of antioxidant enzymes, enhancing plant tolerance to cadmium (Cd) stress. This study aimed to provide guidance that will facilitate future studies of the function of PtOSH1 in the response of plants to Cd stress.</div>
</front>
</TEI>
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<DateCompleted><Year>2020</Year>
<Month>09</Month>
<Day>03</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>09</Month>
<Day>03</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2073-4409</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>9</Volume>
<Issue>1</Issue>
<PubDate><Year>2019</Year>
<Month>12</Month>
<Day>27</Day>
</PubDate>
</JournalIssue>
<Title>Cells</Title>
<ISOAbbreviation>Cells</ISOAbbreviation>
</Journal>
<ArticleTitle>Identification and Characterization of an OSH1 Thiol Reductase from <i>Populus Trichocarpa</i>
.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">E76</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.3390/cells9010076</ELocationID>
<Abstract><AbstractText>Interferon gamma-induced lysosomal thiol reductase (GILT) is abundantly expressed in antigen-presenting cells and participates in the treatment and presentation of antigens by major histocompatibility complex II. Also, GILT catalyzes the reduction of disulfide bonds, which plays an important role in cellular immunity. (1) Background: At present, the studies of GILT have mainly focused on animals. In plants, GILT homologous gene (<i>Arabidopsis thaliana</i>
<i>OSH1</i>
: <i>AtOSH1</i>
) was discovered in the forward screen of mutants with compromised responses to sulphur nutrition. However, the complete properties and functions of poplar OSH1 are unclear. In addition, CdCl<sub>2</sub>
 stress is swiftly engulfing the limited land resources on which humans depend, restricting agricultural production. (2) Methods: A prokaryotic expression system was used to produce recombinant PtOSH1 protein, and Western blotting was performed to identify its activity. In addition, a simplified version of the floral-dip method was used to transform <i>A. thaliana</i>
. (3) Results: Here, we describe the identification and characterization of OSH1 from <i>Populus trichocarpa</i>
. The deduced PtOSH1 sequence contained CQHGX2ECX2NX4C and CXXC motifs. The transcript level of <i>PtOSH1</i>
 was increased by cadmium (Cd) treatment. In addition, recombinant PtOSH1 reduced disulfide bonds. A stress assay showed that <i>PtOSH1</i>
-overexpressing (OE) <i>A. thaliana</i>
 lines had greater resistance to Cd than wild-type (WT) plants. Also, the activities of superoxide dismutase (SOD), peroxidase (POD), and catalase (CAT) in <i>PtOSH1</i>
-OE plants were significantly higher than those in WT <i>A. thaliana</i>
. These results indicate that PtOSH1 likely plays an important role in the response to Cd by regulating the reactive oxygen species (ROS)-scavenging system. (4) Conclusions: PtOSH1 catalyzes the reduction of disulfide bonds and behaves as a sulfhydryl reductase under acidic conditions. The overexpression of <i>PtOSH1</i>
 in <i>A. thaliana</i>
 promoted root development, fresh weight, and dry weight; upregulated the expression levels of ROS scavenging-related genes; and improved the activity of antioxidant enzymes, enhancing plant tolerance to cadmium (Cd) stress. This study aimed to provide guidance that will facilitate future studies of the function of PtOSH1 in the response of plants to Cd stress.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wei</LastName>
<ForeName>Hui</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Zhou</LastName>
<ForeName>Jie</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>Jiangsu Academy of Forestry, Nanjing 211153, China.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Xu</LastName>
<ForeName>Chen</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Jiangsu Provincial Key Construction Laboratory of Special Biomass Resource Utilization, Nanjing Key Laboratory of Quality and Safety of Agricultural Products, Nanjing Xiaozhuang University, Nanjing 211171, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Movahedi</LastName>
<ForeName>Ali</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sun</LastName>
<ForeName>Weibo</ForeName>
<Initials>W</Initials>
<AffiliationInfo><Affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Dawei</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhuge</LastName>
<ForeName>Qiang</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>Co-Innovation Center for Sustainable Forestry in Southern China, Key Laboratory of Forest Genetics & Biotechnology, Ministry of Education, College of Biology and the Environment, Nanjing Forestry University, Nanjing 210037, China.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>BM2018022-01</GrantID>
<Agency>the Research Program of Jiangsu Academy of Forestry</Agency>
<Country>International</Country>
</Grant>
</GrantList>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2019</Year>
<Month>12</Month>
<Day>27</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Switzerland</Country>
<MedlineTA>Cells</MedlineTA>
<NlmUniqueID>101600052</NlmUniqueID>
<ISSNLinking>2073-4409</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 1.8.-</RegistryNumber>
<NameOfSubstance UI="D050862">Oxidoreductases Acting on Sulfur Group Donors</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016366" MajorTopicYN="N">Open Reading Frames</DescriptorName>
</MeshHeading>
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<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
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<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D030821" MajorTopicYN="N">Plants, Genetically Modified</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000145" MajorTopicYN="N">classification</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013312" MajorTopicYN="N">Stress, Physiological</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">GILT</Keyword>
<Keyword MajorTopicYN="Y">Populus trichocarpa</Keyword>
<Keyword MajorTopicYN="Y">PtOSH1</Keyword>
<Keyword MajorTopicYN="Y">ROS-scavenging system</Keyword>
<Keyword MajorTopicYN="Y">cadmium</Keyword>
<Keyword MajorTopicYN="Y">disulfide bond</Keyword>
</KeywordList>
<CoiStatement>The authors declare conflicts of interest.</CoiStatement>
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<Day>24</Day>
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<affiliations><list><country><li>République populaire de Chine</li>
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<tree><country name="République populaire de Chine"><noRegion><name sortKey="Wei, Hui" sort="Wei, Hui" uniqKey="Wei H" first="Hui" last="Wei">Hui Wei</name>
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<name sortKey="Li, Dawei" sort="Li, Dawei" uniqKey="Li D" first="Dawei" last="Li">Dawei Li</name>
<name sortKey="Movahedi, Ali" sort="Movahedi, Ali" uniqKey="Movahedi A" first="Ali" last="Movahedi">Ali Movahedi</name>
<name sortKey="Sun, Weibo" sort="Sun, Weibo" uniqKey="Sun W" first="Weibo" last="Sun">Weibo Sun</name>
<name sortKey="Xu, Chen" sort="Xu, Chen" uniqKey="Xu C" first="Chen" last="Xu">Chen Xu</name>
<name sortKey="Xu, Chen" sort="Xu, Chen" uniqKey="Xu C" first="Chen" last="Xu">Chen Xu</name>
<name sortKey="Zhou, Jie" sort="Zhou, Jie" uniqKey="Zhou J" first="Jie" last="Zhou">Jie Zhou</name>
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Identification and Characterization of an OSH1 Thiol Reductase from Populus Trichocarpa.

Identification and Characterization of an OSH1 Thiol Reductase from Populus Trichocarpa.

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