Sulphite oxidase as key enzyme for protecting plants against sulphur dioxide.
Identifieur interne : 003A71 ( Main/Exploration ); précédent : 003A70; suivant : 003A72Sulphite oxidase as key enzyme for protecting plants against sulphur dioxide.
Auteurs : Christina Lang [Allemagne] ; Jennifer Popko ; Markus Wirtz ; Rüdiger Hell ; Cornelia Herschbach ; Jürgen Kreuzwieser ; Heinz Rennenberg ; Ralf R. Mendel ; Robert H NschSource :
- Plant, cell & environment [ 0140-7791 ] ; 2007.
Descripteurs français
- KwdFr :
- Adaptation biologique (MeSH), Arabidopsis (effets des médicaments et des substances chimiques), Arabidopsis (enzymologie), Arabidopsis (génétique), Dioxyde de soufre (pharmacologie), Glucuronidase (analyse), Interférence par ARN (MeSH), Mutagenèse dirigée (MeSH), Phénotype (MeSH), Populus (effets des médicaments et des substances chimiques), Populus (enzymologie), Populus (génétique), Régulation de l'expression des gènes végétaux (MeSH), Régulation négative (MeSH), Sulfite oxidase (antagonistes et inhibiteurs), Sulfite oxidase (génétique), Sulfite oxidase (physiologie), Tabac (effets des médicaments et des substances chimiques), Tabac (enzymologie), Tabac (génétique).
- MESH :
- analyse : Glucuronidase.
- antagonistes et inhibiteurs : Sulfite oxidase.
- effets des médicaments et des substances chimiques : Arabidopsis, Populus, Tabac.
- enzymologie : Arabidopsis, Populus, Tabac.
- génétique : Arabidopsis, Populus, Sulfite oxidase, Tabac.
- pharmacologie : Dioxyde de soufre.
- physiologie : Sulfite oxidase.
- Adaptation biologique, Interférence par ARN, Mutagenèse dirigée, Phénotype, Régulation de l'expression des gènes végétaux, Régulation négative.
English descriptors
- KwdEn :
- Adaptation, Biological (MeSH), Arabidopsis (drug effects), Arabidopsis (enzymology), Arabidopsis (genetics), Down-Regulation (MeSH), Gene Expression Regulation, Plant (MeSH), Glucuronidase (analysis), Mutagenesis, Site-Directed (MeSH), Phenotype (MeSH), Populus (drug effects), Populus (enzymology), Populus (genetics), RNA Interference (MeSH), Sulfite Oxidase (antagonists & inhibitors), Sulfite Oxidase (genetics), Sulfite Oxidase (physiology), Sulfur Dioxide (pharmacology), Tobacco (drug effects), Tobacco (enzymology), Tobacco (genetics).
- MESH :
- chemical , analysis : Glucuronidase.
- chemical , antagonists & inhibitors : Sulfite Oxidase.
- drug effects : Arabidopsis, Populus, Tobacco.
- enzymology : Arabidopsis, Populus, Tobacco.
- genetics : Arabidopsis, Populus, Sulfite Oxidase, Tobacco.
- chemical , pharmacology : Sulfur Dioxide.
- chemical , physiology : Sulfite Oxidase.
- Adaptation, Biological, Down-Regulation, Gene Expression Regulation, Plant, Mutagenesis, Site-Directed, Phenotype, RNA Interference.
Abstract
Sulphur dioxide (SO(2)) is known as a strongly damaging air pollutant. After conversion to sulphite in aqueous solution, it becomes a strong nucleophilic agent that attacks numerous compounds in the cell. Therefore, plants have developed a mechanism to control sulphite levels. Recently, we have cloned and characterized the enzyme sulphite oxidase (SO) from Arabidopsis thaliana. Yet, its physiological role remained unclear. Here, we describe results demonstrating that SO is essential for detoxifying excessive amounts of sulphite in the cell which is important for the survival of the plant. T-DNA-tagged A. thaliana plants lacking the enzyme showed a decrease in vitality during SO(2) fumigation and a change in their S-metabolites. The same was found with RNA-interference (RNAi) plants that were generated for tobacco. On the contrary, over-expression of SO helped the plant to survive SO(2) concentrations that are detrimental for non-transformed wild-type (WT) plants, as was shown with poplar plants which are known to be particularly sensitive to SO(2). Fumigation induced the expression of the enzyme as demonstrated by promoter-reporter gene fusion, by immunoblot analysis of SO-protein and by induction of enzyme activity. This implies that SO, as an otherwise constitutively expressed protein, is under additional control by SO(2) in the environment.
DOI: 10.1111/j.1365-3040.2006.01632.x
PubMed: 17324231
Affiliations:
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Mendel</name></author><author><name sortKey="H Nsch, Robert" sort="H Nsch, Robert" uniqKey="H Nsch R" first="Robert" last="H Nsch">Robert H Nsch</name></author></analytic><series><title level="j">Plant, cell & environment</title><idno type="ISSN">0140-7791</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptation, Biological (MeSH)</term><term>Arabidopsis (drug effects)</term><term>Arabidopsis (enzymology)</term><term>Arabidopsis (genetics)</term><term>Down-Regulation (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Glucuronidase (analysis)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Phenotype (MeSH)</term><term>Populus (drug effects)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>RNA Interference (MeSH)</term><term>Sulfite Oxidase (antagonists & inhibitors)</term><term>Sulfite Oxidase (genetics)</term><term>Sulfite Oxidase (physiology)</term><term>Sulfur Dioxide (pharmacology)</term><term>Tobacco (drug effects)</term><term>Tobacco (enzymology)</term><term>Tobacco (genetics)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adaptation biologique (MeSH)</term><term>Arabidopsis (effets des médicaments et des substances chimiques)</term><term>Arabidopsis (enzymologie)</term><term>Arabidopsis (génétique)</term><term>Dioxyde de soufre (pharmacologie)</term><term>Glucuronidase (analyse)</term><term>Interférence par ARN (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Phénotype (MeSH)</term><term>Populus (effets des médicaments et des substances chimiques)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Régulation négative (MeSH)</term><term>Sulfite oxidase (antagonistes et inhibiteurs)</term><term>Sulfite oxidase (génétique)</term><term>Sulfite oxidase (physiologie)</term><term>Tabac (effets des médicaments et des substances chimiques)</term><term>Tabac (enzymologie)</term><term>Tabac (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Glucuronidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Sulfite Oxidase</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Glucuronidase</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Sulfite oxidase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Arabidopsis</term><term>Populus</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Arabidopsis</term><term>Populus</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Arabidopsis</term><term>Populus</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Arabidopsis</term><term>Populus</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Arabidopsis</term><term>Populus</term><term>Sulfite Oxidase</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Arabidopsis</term><term>Populus</term><term>Sulfite oxidase</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Dioxyde de soufre</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sulfur Dioxide</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Sulfite oxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Sulfite Oxidase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adaptation, Biological</term><term>Down-Regulation</term><term>Gene Expression Regulation, Plant</term><term>Mutagenesis, Site-Directed</term><term>Phenotype</term><term>RNA Interference</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adaptation biologique</term><term>Interférence par ARN</term><term>Mutagenèse dirigée</term><term>Phénotype</term><term>Régulation de l'expression des gènes végétaux</term><term>Régulation négative</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Sulphur dioxide (SO(2)) is known as a strongly damaging air pollutant. After conversion to sulphite in aqueous solution, it becomes a strong nucleophilic agent that attacks numerous compounds in the cell. Therefore, plants have developed a mechanism to control sulphite levels. Recently, we have cloned and characterized the enzyme sulphite oxidase (SO) from Arabidopsis thaliana. Yet, its physiological role remained unclear. Here, we describe results demonstrating that SO is essential for detoxifying excessive amounts of sulphite in the cell which is important for the survival of the plant. T-DNA-tagged A. thaliana plants lacking the enzyme showed a decrease in vitality during SO(2) fumigation and a change in their S-metabolites. The same was found with RNA-interference (RNAi) plants that were generated for tobacco. On the contrary, over-expression of SO helped the plant to survive SO(2) concentrations that are detrimental for non-transformed wild-type (WT) plants, as was shown with poplar plants which are known to be particularly sensitive to SO(2). Fumigation induced the expression of the enzyme as demonstrated by promoter-reporter gene fusion, by immunoblot analysis of SO-protein and by induction of enzyme activity. This implies that SO, as an otherwise constitutively expressed protein, is under additional control by SO(2) in the environment.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17324231</PMID><DateCompleted><Year>2007</Year><Month>07</Month><Day>18</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0140-7791</ISSN><JournalIssue CitedMedium="Print"><Volume>30</Volume><Issue>4</Issue><PubDate><Year>2007</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Plant, cell & environment</Title><ISOAbbreviation>Plant Cell Environ</ISOAbbreviation></Journal><ArticleTitle>Sulphite oxidase as key enzyme for protecting plants against sulphur dioxide.</ArticleTitle><Pagination><MedlinePgn>447-55</MedlinePgn></Pagination><Abstract><AbstractText>Sulphur dioxide (SO(2)) is known as a strongly damaging air pollutant. After conversion to sulphite in aqueous solution, it becomes a strong nucleophilic agent that attacks numerous compounds in the cell. Therefore, plants have developed a mechanism to control sulphite levels. Recently, we have cloned and characterized the enzyme sulphite oxidase (SO) from Arabidopsis thaliana. Yet, its physiological role remained unclear. Here, we describe results demonstrating that SO is essential for detoxifying excessive amounts of sulphite in the cell which is important for the survival of the plant. T-DNA-tagged A. thaliana plants lacking the enzyme showed a decrease in vitality during SO(2) fumigation and a change in their S-metabolites. The same was found with RNA-interference (RNAi) plants that were generated for tobacco. On the contrary, over-expression of SO helped the plant to survive SO(2) concentrations that are detrimental for non-transformed wild-type (WT) plants, as was shown with poplar plants which are known to be particularly sensitive to SO(2). Fumigation induced the expression of the enzyme as demonstrated by promoter-reporter gene fusion, by immunoblot analysis of SO-protein and by induction of enzyme activity. This implies that SO, as an otherwise constitutively expressed protein, is under additional control by SO(2) in the environment.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lang</LastName><ForeName>Christina</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Institut für Pflanzenbiologie, Technische Universität Braunschweig, Humboldtstrasse 1, D-38106 Braunschweig, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Popko</LastName><ForeName>Jennifer</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wirtz</LastName><ForeName>Markus</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Hell</LastName><ForeName>Rüdiger</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Herschbach</LastName><ForeName>Cornelia</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Kreuzwieser</LastName><ForeName>Jürgen</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Rennenberg</LastName><ForeName>Heinz</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Mendel</LastName><ForeName>Ralf R</ForeName><Initials>RR</Initials></Author><Author ValidYN="Y"><LastName>Hänsch</LastName><ForeName>Robert</ForeName><Initials>R</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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Cell Environ</MedlineTA><NlmUniqueID>9309004</NlmUniqueID><ISSNLinking>0140-7791</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0UZA3422Q4</RegistryNumber><NameOfSubstance UI="D013458">Sulfur Dioxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.3.1</RegistryNumber><NameOfSubstance UI="D050876">Sulfite Oxidase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.2.1.31</RegistryNumber><NameOfSubstance UI="D005966">Glucuronidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000220" MajorTopicYN="N">Adaptation, Biological</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015536" MajorTopicYN="N">Down-Regulation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005966" MajorTopicYN="N">Glucuronidase</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050876" MajorTopicYN="N">Sulfite Oxidase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013458" MajorTopicYN="N">Sulfur Dioxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2007</Year><Month>2</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>7</Month><Day>19</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2007</Year><Month>2</Month><Day>28</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17324231</ArticleId><ArticleId IdType="pii">PCE1632</ArticleId><ArticleId IdType="doi">10.1111/j.1365-3040.2006.01632.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="H Nsch, Robert" sort="H Nsch, Robert" uniqKey="H Nsch R" first="Robert" last="H Nsch">Robert H Nsch</name><name sortKey="Hell, Rudiger" sort="Hell, Rudiger" uniqKey="Hell R" first="Rüdiger" last="Hell">Rüdiger Hell</name><name sortKey="Herschbach, Cornelia" sort="Herschbach, Cornelia" uniqKey="Herschbach C" first="Cornelia" last="Herschbach">Cornelia Herschbach</name><name sortKey="Kreuzwieser, Jurgen" sort="Kreuzwieser, Jurgen" uniqKey="Kreuzwieser J" first="Jürgen" last="Kreuzwieser">Jürgen Kreuzwieser</name><name sortKey="Mendel, Ralf R" sort="Mendel, Ralf R" uniqKey="Mendel R" first="Ralf R" last="Mendel">Ralf R. Mendel</name><name sortKey="Popko, Jennifer" sort="Popko, Jennifer" uniqKey="Popko J" first="Jennifer" last="Popko">Jennifer Popko</name><name sortKey="Rennenberg, Heinz" sort="Rennenberg, Heinz" uniqKey="Rennenberg H" first="Heinz" last="Rennenberg">Heinz Rennenberg</name><name sortKey="Wirtz, Markus" sort="Wirtz, Markus" uniqKey="Wirtz M" first="Markus" last="Wirtz">Markus Wirtz</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Lang, Christina" sort="Lang, Christina" uniqKey="Lang C" first="Christina" last="Lang">Christina Lang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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