A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance.
Identifieur interne : 001A00 ( Main/Exploration ); précédent : 001999; suivant : 001A01A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance.
Auteurs : Shuta Asai [Japon] ; Keisuke Mase ; Hirofumi YoshiokaSource :
- The Plant journal : for cell and molecular biology [ 1365-313X ] ; 2010.
Descripteurs français
- KwdFr :
- Banque de gènes (MeSH), Espèces réactives de l'oxygène (métabolisme), Extinction de l'expression des gènes (MeSH), Flavines (biosynthèse), Gènes de plante (MeSH), Immunité innée (MeSH), Intramolecular transferases (génétique), Intramolecular transferases (métabolisme), Monoxyde d'azote (métabolisme), Mort cellulaire (MeSH), Mutagenèse dirigée (MeSH), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Régulation de l'expression des gènes végétaux (MeSH), Tabac (enzymologie), Tabac (génétique), Tabac (immunologie).
- MESH :
- biosynthèse : Flavines.
- enzymologie : Tabac.
- génétique : Intramolecular transferases, Protéines recombinantes, Protéines végétales, Tabac.
- immunologie : Tabac.
- métabolisme : Espèces réactives de l'oxygène, Intramolecular transferases, Monoxyde d'azote, Protéines recombinantes, Protéines végétales.
- Banque de gènes, Extinction de l'expression des gènes, Gènes de plante, Immunité innée, Mort cellulaire, Mutagenèse dirigée, Régulation de l'expression des gènes végétaux.
English descriptors
- KwdEn :
- Cell Death (MeSH), Flavins (biosynthesis), Gene Expression Regulation, Plant (MeSH), Gene Library (MeSH), Gene Silencing (MeSH), Genes, Plant (MeSH), Immunity, Innate (MeSH), Intramolecular Transferases (genetics), Intramolecular Transferases (metabolism), Mutagenesis, Site-Directed (MeSH), Nitric Oxide (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Reactive Oxygen Species (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Tobacco (enzymology), Tobacco (genetics), Tobacco (immunology).
- MESH :
- chemical , biosynthesis : Flavins.
- chemical , genetics : Intramolecular Transferases, Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Intramolecular Transferases, Nitric Oxide, Plant Proteins, Reactive Oxygen Species, Recombinant Proteins.
- enzymology : Tobacco.
- genetics : Tobacco.
- immunology : Tobacco.
- Cell Death, Gene Expression Regulation, Plant, Gene Library, Gene Silencing, Genes, Plant, Immunity, Innate, Mutagenesis, Site-Directed.
Abstract
Nitric oxide (NO) and reactive oxygen species (ROS) play key roles in plant immunity. However, the regulatory mechanisms of the production of these radicals are not fully understood. Hypersensitive response (HR) cell death requires the simultaneous and balanced production of NO and ROS. In this study we indentified NbRibAencoding a bifunctional enzyme, guanosine triphosphate cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate synthase, which participates in the biosynthesis of flavin, by screening genes related to mitogen-activated protein kinase-mediated cell death, using virus-induced gene silencing. Levels of endogenous riboflavin and its derivatives, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are important prosthetic groups for several enzymes participating in redox reactions, decreased in NbRibA-silenced Nicotiana benthamiana. Silencing NbRibA compromised not only HR cell death, but also the NO and ROS production induced by INF1 elicitin and a constitutively active form of NbMEK2 (NbMEK2DD), and also induced high susceptibility to oomycete Phytophthora infestans and ascomycete Colletotrichum orbiculare. Compromised radical production and HR cell death induced by INF1 in NbRibA-silenced leaves were rescued by adding riboflavin, FMN or FAD. These results indicate that flavin biosynthesis participates in regulating NO and ROS production, and HR cell death.
DOI: 10.1111/j.0960-7412.2010.04206.x
PubMed: 20230506
Affiliations:
Links toward previous steps (curation, corpus...)
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type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Death (MeSH)</term><term>Flavins (biosynthesis)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Gene Library (MeSH)</term><term>Gene Silencing (MeSH)</term><term>Genes, Plant (MeSH)</term><term>Immunity, Innate (MeSH)</term><term>Intramolecular Transferases (genetics)</term><term>Intramolecular Transferases (metabolism)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Nitric Oxide (metabolism)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Reactive Oxygen Species (metabolism)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (metabolism)</term><term>Tobacco (enzymology)</term><term>Tobacco (genetics)</term><term>Tobacco (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Banque de gènes (MeSH)</term><term>Espèces réactives de l'oxygène (métabolisme)</term><term>Extinction de l'expression des gènes (MeSH)</term><term>Flavines (biosynthèse)</term><term>Gènes de plante (MeSH)</term><term>Immunité innée (MeSH)</term><term>Intramolecular transferases (génétique)</term><term>Intramolecular transferases (métabolisme)</term><term>Monoxyde d'azote (métabolisme)</term><term>Mort cellulaire (MeSH)</term><term>Mutagenèse dirigée (MeSH)</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (métabolisme)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (métabolisme)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Tabac (enzymologie)</term><term>Tabac (génétique)</term><term>Tabac (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Flavins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Intramolecular Transferases</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Intramolecular Transferases</term><term>Nitric Oxide</term><term>Plant Proteins</term><term>Reactive Oxygen Species</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Flavines</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Intramolecular transferases</term><term>Protéines recombinantes</term><term>Protéines végétales</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="immunologie" 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type="abstract" xml:lang="en">Nitric oxide (NO) and reactive oxygen species (ROS) play key roles in plant immunity. However, the regulatory mechanisms of the production of these radicals are not fully understood. Hypersensitive response (HR) cell death requires the simultaneous and balanced production of NO and ROS. In this study we indentified NbRibAencoding a bifunctional enzyme, guanosine triphosphate cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate synthase, which participates in the biosynthesis of flavin, by screening genes related to mitogen-activated protein kinase-mediated cell death, using virus-induced gene silencing. Levels of endogenous riboflavin and its derivatives, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are important prosthetic groups for several enzymes participating in redox reactions, decreased in NbRibA-silenced Nicotiana benthamiana. Silencing NbRibA compromised not only HR cell death, but also the NO and ROS production induced by INF1 elicitin and a constitutively active form of NbMEK2 (NbMEK2DD), and also induced high susceptibility to oomycete Phytophthora infestans and ascomycete Colletotrichum orbiculare. Compromised radical production and HR cell death induced by INF1 in NbRibA-silenced leaves were rescued by adding riboflavin, FMN or FAD. These results indicate that flavin biosynthesis participates in regulating NO and ROS production, and HR cell death.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20230506</PMID><DateCompleted><Year>2010</Year><Month>09</Month><Day>27</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1365-313X</ISSN><JournalIssue CitedMedium="Internet"><Volume>62</Volume><Issue>6</Issue><PubDate><Year>2010</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>A key enzyme for flavin synthesis is required for nitric oxide and reactive oxygen species production in disease resistance.</ArticleTitle><Pagination><MedlinePgn>911-24</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/j.0960-7412.2010.04206.x</ELocationID><Abstract><AbstractText>Nitric oxide (NO) and reactive oxygen species (ROS) play key roles in plant immunity. However, the regulatory mechanisms of the production of these radicals are not fully understood. Hypersensitive response (HR) cell death requires the simultaneous and balanced production of NO and ROS. In this study we indentified NbRibAencoding a bifunctional enzyme, guanosine triphosphate cyclohydrolase II/3,4-dihydroxy-2-butanone-4-phosphate synthase, which participates in the biosynthesis of flavin, by screening genes related to mitogen-activated protein kinase-mediated cell death, using virus-induced gene silencing. Levels of endogenous riboflavin and its derivatives, flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which are important prosthetic groups for several enzymes participating in redox reactions, decreased in NbRibA-silenced Nicotiana benthamiana. Silencing NbRibA compromised not only HR cell death, but also the NO and ROS production induced by INF1 elicitin and a constitutively active form of NbMEK2 (NbMEK2DD), and also induced high susceptibility to oomycete Phytophthora infestans and ascomycete Colletotrichum orbiculare. Compromised radical production and HR cell death induced by INF1 in NbRibA-silenced leaves were rescued by adding riboflavin, FMN or FAD. These results indicate that flavin biosynthesis participates in regulating NO and ROS production, and HR cell death.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Asai</LastName><ForeName>Shuta</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Laboratory of Defense in Plant-Pathogen Interactions, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya 464-8601, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mase</LastName><ForeName>Keisuke</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Yoshioka</LastName><ForeName>Hirofumi</ForeName><Initials>H</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>England</Country><MedlineTA>Plant J</MedlineTA><NlmUniqueID>9207397</NlmUniqueID><ISSNLinking>0960-7412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005415">Flavins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017382">Reactive Oxygen Species</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber><NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.4.-</RegistryNumber><NameOfSubstance UI="D019751">Intramolecular Transferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.4.-</RegistryNumber><NameOfSubstance UI="C066493">L-3,4-dihydroxy-2-butanone-4-phosphate synthase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D016923" MajorTopicYN="N">Cell Death</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005415" MajorTopicYN="N">Flavins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015723" MajorTopicYN="N">Gene Library</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020868" MajorTopicYN="N">Gene Silencing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017343" MajorTopicYN="N">Genes, Plant</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007113" MajorTopicYN="N">Immunity, Innate</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019751" MajorTopicYN="N">Intramolecular Transferases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016297" MajorTopicYN="N">Mutagenesis, Site-Directed</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009569" MajorTopicYN="N">Nitric Oxide</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></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="D014026" MajorTopicYN="N">Tobacco</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>3</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>3</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>9</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20230506</ArticleId><ArticleId IdType="pii">TPJ4206</ArticleId><ArticleId IdType="doi">10.1111/j.0960-7412.2010.04206.x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Mase, Keisuke" sort="Mase, Keisuke" uniqKey="Mase K" first="Keisuke" last="Mase">Keisuke Mase</name><name sortKey="Yoshioka, Hirofumi" sort="Yoshioka, Hirofumi" uniqKey="Yoshioka H" first="Hirofumi" last="Yoshioka">Hirofumi Yoshioka</name></noCountry><country name="Japon"><noRegion><name sortKey="Asai, Shuta" sort="Asai, Shuta" uniqKey="Asai S" first="Shuta" last="Asai">Shuta Asai</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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