Redox-dependent functional switching of plant proteins accompanying with their structural changes.
Identifieur interne : 000721 ( Main/Exploration ); précédent : 000720; suivant : 000722Redox-dependent functional switching of plant proteins accompanying with their structural changes.
Auteurs : Yong Hun Chi [Corée du Sud] ; Seol Ki Paeng ; Min Ji Kim ; Gwang Yong Hwang ; Sarah Mae B. Melencion ; Hun Taek Oh ; Sang Yeol LeeSource :
- Frontiers in plant science [ 1664-462X ] ; 2013.
Abstract
Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins.
DOI: 10.3389/fpls.2013.00277
PubMed: 23898340
PubMed Central: PMC3724125
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Redox-dependent functional switching of plant proteins accompanying with their structural changes.</title><author><name sortKey="Chi, Yong Hun" sort="Chi, Yong Hun" uniqKey="Chi Y" first="Yong Hun" last="Chi">Yong Hun Chi</name><affiliation wicri:level="1"><nlm:affiliation>Division of Applied Life Sciences, Gyeongsang National University Jinju, Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Division of Applied Life Sciences, Gyeongsang National University Jinju</wicri:regionArea><wicri:noRegion>Gyeongsang National University Jinju</wicri:noRegion></affiliation></author><author><name sortKey="Paeng, Seol Ki" sort="Paeng, Seol Ki" uniqKey="Paeng S" first="Seol Ki" last="Paeng">Seol Ki Paeng</name></author><author><name sortKey="Kim, Min Ji" sort="Kim, Min Ji" uniqKey="Kim M" first="Min Ji" last="Kim">Min Ji Kim</name></author><author><name sortKey="Hwang, Gwang Yong" sort="Hwang, Gwang Yong" uniqKey="Hwang G" first="Gwang Yong" last="Hwang">Gwang Yong Hwang</name></author><author><name sortKey="Melencion, Sarah Mae B" sort="Melencion, Sarah Mae B" uniqKey="Melencion S" first="Sarah Mae B" last="Melencion">Sarah Mae B. Melencion</name></author><author><name sortKey="Oh, Hun Taek" sort="Oh, Hun Taek" uniqKey="Oh H" first="Hun Taek" last="Oh">Hun Taek Oh</name></author><author><name sortKey="Lee, Sang Yeol" sort="Lee, Sang Yeol" uniqKey="Lee S" first="Sang Yeol" last="Lee">Sang Yeol Lee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23898340</idno><idno type="pmid">23898340</idno><idno type="doi">10.3389/fpls.2013.00277</idno><idno type="pmc">PMC3724125</idno><idno type="wicri:Area/Main/Corpus">000719</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000719</idno><idno type="wicri:Area/Main/Curation">000719</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000719</idno><idno type="wicri:Area/Main/Exploration">000719</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Redox-dependent functional switching of plant proteins accompanying with their structural changes.</title><author><name sortKey="Chi, Yong Hun" sort="Chi, Yong Hun" uniqKey="Chi Y" first="Yong Hun" last="Chi">Yong Hun Chi</name><affiliation wicri:level="1"><nlm:affiliation>Division of Applied Life Sciences, Gyeongsang National University Jinju, Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Division of Applied Life Sciences, Gyeongsang National University Jinju</wicri:regionArea><wicri:noRegion>Gyeongsang National University Jinju</wicri:noRegion></affiliation></author><author><name sortKey="Paeng, Seol Ki" sort="Paeng, Seol Ki" uniqKey="Paeng S" first="Seol Ki" last="Paeng">Seol Ki Paeng</name></author><author><name sortKey="Kim, Min Ji" sort="Kim, Min Ji" uniqKey="Kim M" first="Min Ji" last="Kim">Min Ji Kim</name></author><author><name sortKey="Hwang, Gwang Yong" sort="Hwang, Gwang Yong" uniqKey="Hwang G" first="Gwang Yong" last="Hwang">Gwang Yong Hwang</name></author><author><name sortKey="Melencion, Sarah Mae B" sort="Melencion, Sarah Mae B" uniqKey="Melencion S" first="Sarah Mae B" last="Melencion">Sarah Mae B. Melencion</name></author><author><name sortKey="Oh, Hun Taek" sort="Oh, Hun Taek" uniqKey="Oh H" first="Hun Taek" last="Oh">Hun Taek Oh</name></author><author><name sortKey="Lee, Sang Yeol" sort="Lee, Sang Yeol" uniqKey="Lee S" first="Sang Yeol" last="Lee">Sang Yeol Lee</name></author></analytic><series><title level="j">Frontiers in plant science</title><idno type="ISSN">1664-462X</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins. </div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">23898340</PMID><DateCompleted><Year>2013</Year><Month>07</Month><Day>30</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>4</Volume><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle>Redox-dependent functional switching of plant proteins accompanying with their structural changes.</ArticleTitle><Pagination><MedlinePgn>277</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2013.00277</ELocationID><Abstract><AbstractText>Reactive oxygen species (ROS) can be generated during the course of normal aerobic metabolism or when an organism is exposed to a variety of stress conditions. It can cause a widespread damage to intracellular macromolecules and play a causal role in many degenerative diseases. Like other aerobic organisms plants are also equipped with a wide range of antioxidant redox proteins, such as superoxide dismutase, catalase, glutaredoxin, thioredoxin (Trx), Trx reductase, protein disulfide reductase, and other kinds of peroxidases that are usually significant in preventing harmful effects of ROS. To defend plant cells in response to stimuli, a part of redox proteins have shown to play multiple functions through the post-translational modification with a redox-dependent manner. For the alternative switching of their cellular functions, the redox proteins change their protein structures from low molecular weight to high molecular weight (HMW) protein complexes depending on the external stress. The HMW proteins are reported to act as molecular chaperone, which enable the plants to enhance their stress tolerance. In addition, some transcription factors and co-activators have function responding to environmental stresses by redox-dependent structural changes. This review describes the molecular mechanism and physiological significance of the redox proteins, transcription factors and co-activators to protect the plants from environmental stresses through the redox-dependent structural and functional switching of the plant redox proteins. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chi</LastName><ForeName>Yong Hun</ForeName><Initials>YH</Initials><AffiliationInfo><Affiliation>Division of Applied Life Sciences, Gyeongsang National University Jinju, Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Paeng</LastName><ForeName>Seol Ki</ForeName><Initials>SK</Initials></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Min Ji</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Gwang Yong</ForeName><Initials>GY</Initials></Author><Author ValidYN="Y"><LastName>Melencion</LastName><ForeName>Sarah Mae B</ForeName><Initials>SM</Initials></Author><Author ValidYN="Y"><LastName>Oh</LastName><ForeName>Hun Taek</ForeName><Initials>HT</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Sang Yeol</ForeName><Initials>SY</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>07</Month><Day>26</Day></ArticleDate></Article><MedlineJournalInfo><Country>Switzerland</Country><MedlineTA>Front Plant Sci</MedlineTA><NlmUniqueID>101568200</NlmUniqueID><ISSNLinking>1664-462X</ISSNLinking></MedlineJournalInfo><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">external stress</Keyword><Keyword MajorTopicYN="N">molecular chaperone</Keyword><Keyword MajorTopicYN="N">multiple functions</Keyword><Keyword MajorTopicYN="N">redox proteins</Keyword><Keyword MajorTopicYN="N">structural and functional 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Melencion</name><name sortKey="Oh, Hun Taek" sort="Oh, Hun Taek" uniqKey="Oh H" first="Hun Taek" last="Oh">Hun Taek Oh</name><name sortKey="Paeng, Seol Ki" sort="Paeng, Seol Ki" uniqKey="Paeng S" first="Seol Ki" last="Paeng">Seol Ki Paeng</name></noCountry><country name="Corée du Sud"><noRegion><name sortKey="Chi, Yong Hun" sort="Chi, Yong Hun" uniqKey="Chi Y" first="Yong Hun" last="Chi">Yong Hun Chi</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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