PhytophthoraV1, Main, Exploration, bibRecord, 001114

Dynamic changes in the subcellular distribution of the tobacco ROS-producing enzyme RBOHD in response to the oomycete elicitor cryptogein.

Identifieur interne : 001114 ( Main/Exploration ); précédent : 001113; suivant : 001115

Dynamic changes in the subcellular distribution of the tobacco ROS-producing enzyme RBOHD in response to the oomycete elicitor cryptogein.

Auteurs : Elodie Noirot [France] ; Christophe Der [France] ; Jeannine Lherminier [France] ; Franck Robert [France] ; Pavla Moricova [République tchèque] ; Kiên Kiêu [France] ; Nathalie Leborgne-Castel [France] ; Françoise Simon-Plas [France] ; Karim Bouhidel [France]

Source :

Journal of experimental botany [ 1460-2431 ] ; 2014.

RBID : pubmed:24987013

Descripteurs français

KwdFr :
- Espèces réactives de l'oxygène (métabolisme), Membrane cellulaire (métabolisme), Microscopie confocale (MeSH), Microscopie électronique à transmission (MeSH), NADPH oxidase (génétique), NADPH oxidase (métabolisme), Phytophthora (physiologie), Protéines fongiques (métabolisme), Protéines végétales (génétique), Protéines végétales (métabolisme), Réaction de polymérisation en chaine en temps réel (MeSH), Tabac (génétique), Tabac (microbiologie), Tabac (métabolisme).
MESH :
- génétique : NADPH oxidase, Protéines végétales, Tabac.
- microbiologie : Tabac.
- métabolisme : Espèces réactives de l'oxygène, Membrane cellulaire, NADPH oxidase, Protéines fongiques, Protéines végétales, Tabac.
- physiologie : Phytophthora.
- Microscopie confocale, Microscopie électronique à transmission, Réaction de polymérisation en chaine en temps réel.

English descriptors

KwdEn :
- Cell Membrane (metabolism), Fungal Proteins (metabolism), Microscopy, Confocal (MeSH), Microscopy, Electron, Transmission (MeSH), NADPH Oxidases (genetics), NADPH Oxidases (metabolism), Phytophthora (physiology), Plant Proteins (genetics), Plant Proteins (metabolism), Reactive Oxygen Species (metabolism), Real-Time Polymerase Chain Reaction (MeSH), Tobacco (genetics), Tobacco (metabolism), Tobacco (microbiology).
MESH :
- chemical , genetics : NADPH Oxidases, Plant Proteins.
- chemical , metabolism : Fungal Proteins, NADPH Oxidases, Plant Proteins, Reactive Oxygen Species.
- genetics : Tobacco.
- metabolism : Cell Membrane, Tobacco.
- microbiology : Tobacco.
- physiology : Phytophthora.
- Microscopy, Confocal, Microscopy, Electron, Transmission, Real-Time Polymerase Chain Reaction.

Abstract

Plant NADPH oxidases, also known as respiratory burst oxidase homologues (RBOHs), have been identified as a major source of reactive oxygen species (ROS) during plant-microbe interactions. The subcellular localization of the tobacco (Nicotiana tabacum) ROS-producing enzyme RBOHD was examined in Bright Yellow-2 cells before and after elicitation with the oomycete protein cryptogein using electron and confocal microscopy. The plasma membrane (PM) localization of RBOHD was confirmed and immuno-electron microscopy on purified PM vesicles revealed its distribution in clusters. The presence of the protein fused to GFP was also seen in intracellular compartments, mainly Golgi cisternae. Cryptogein induced, within 1h, a 1.5-fold increase in RBOHD abundance at the PM and a concomitant decrease in the internal compartments. Use of cycloheximide revealed that most of the proteins targeted to the PM upon elicitation were not newly synthesized but may originate from the Golgi pool. ROS accumulation preceded RBOHD transcript- and protein-upregulation, indicating that ROS resulted from the activation of a PM-resident pool of enzymes, and that enzymes newly addressed to the PM were inactive. Taken together, the results indicate that control of RBOH abundance and subcellular localization may play a fundamental role in the mechanism of ROS production.

DOI: 10.1093/jxb/eru265
PubMed: 24987013
PubMed Central: PMC4144778

Affiliations:

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

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Le document en format XML

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<country xml:lang="fr">France</country>
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<country xml:lang="fr">République tchèque</country>
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<country xml:lang="fr">France</country>
<wicri:regionArea>INRA, UR341 Mathématiques et Informatique Appliquées, F-78352 Jouy-en-Josas Cedex</wicri:regionArea>
<placeName><region type="region" nuts="2">Île-de-France</region>
<settlement type="city">Jouy-en-Josas</settlement>
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<country xml:lang="fr">France</country>
<wicri:regionArea>Université de Bourgogne, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex</wicri:regionArea>
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<term>Fungal Proteins (metabolism)</term>
<term>Microscopy, Confocal (MeSH)</term>
<term>Microscopy, Electron, Transmission (MeSH)</term>
<term>NADPH Oxidases (genetics)</term>
<term>NADPH Oxidases (metabolism)</term>
<term>Phytophthora (physiology)</term>
<term>Plant Proteins (genetics)</term>
<term>Plant Proteins (metabolism)</term>
<term>Reactive Oxygen Species (metabolism)</term>
<term>Real-Time Polymerase Chain Reaction (MeSH)</term>
<term>Tobacco (genetics)</term>
<term>Tobacco (metabolism)</term>
<term>Tobacco (microbiology)</term>
</keywords>
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<term>Membrane cellulaire (métabolisme)</term>
<term>Microscopie confocale (MeSH)</term>
<term>Microscopie électronique à transmission (MeSH)</term>
<term>NADPH oxidase (génétique)</term>
<term>NADPH oxidase (métabolisme)</term>
<term>Phytophthora (physiologie)</term>
<term>Protéines fongiques (métabolisme)</term>
<term>Protéines végétales (génétique)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Réaction de polymérisation en chaine en temps réel (MeSH)</term>
<term>Tabac (génétique)</term>
<term>Tabac (microbiologie)</term>
<term>Tabac (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>NADPH Oxidases</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term>
<term>NADPH Oxidases</term>
<term>Plant Proteins</term>
<term>Reactive Oxygen Species</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Tobacco</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>NADPH oxidase</term>
<term>Protéines végétales</term>
<term>Tabac</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Membrane</term>
<term>Tobacco</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Tabac</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Tobacco</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Espèces réactives de l'oxygène</term>
<term>Membrane cellulaire</term>
<term>NADPH oxidase</term>
<term>Protéines fongiques</term>
<term>Protéines végétales</term>
<term>Tabac</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Phytophthora</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Phytophthora</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Microscopy, Confocal</term>
<term>Microscopy, Electron, Transmission</term>
<term>Real-Time Polymerase Chain Reaction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Microscopie confocale</term>
<term>Microscopie électronique à transmission</term>
<term>Réaction de polymérisation en chaine en temps réel</term>
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<front><div type="abstract" xml:lang="en">Plant NADPH oxidases, also known as respiratory burst oxidase homologues (RBOHs), have been identified as a major source of reactive oxygen species (ROS) during plant-microbe interactions. The subcellular localization of the tobacco (Nicotiana tabacum) ROS-producing enzyme RBOHD was examined in Bright Yellow-2 cells before and after elicitation with the oomycete protein cryptogein using electron and confocal microscopy. The plasma membrane (PM) localization of RBOHD was confirmed and immuno-electron microscopy on purified PM vesicles revealed its distribution in clusters. The presence of the protein fused to GFP was also seen in intracellular compartments, mainly Golgi cisternae. Cryptogein induced, within 1h, a 1.5-fold increase in RBOHD abundance at the PM and a concomitant decrease in the internal compartments. Use of cycloheximide revealed that most of the proteins targeted to the PM upon elicitation were not newly synthesized but may originate from the Golgi pool. ROS accumulation preceded RBOHD transcript- and protein-upregulation, indicating that ROS resulted from the activation of a PM-resident pool of enzymes, and that enzymes newly addressed to the PM were inactive. Taken together, the results indicate that control of RBOH abundance and subcellular localization may play a fundamental role in the mechanism of ROS production. </div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24987013</PMID>
<DateCompleted><Year>2015</Year>
<Month>05</Month>
<Day>28</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2431</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>65</Volume>
<Issue>17</Issue>
<PubDate><Year>2014</Year>
<Month>Sep</Month>
</PubDate>
</JournalIssue>
<Title>Journal of experimental botany</Title>
<ISOAbbreviation>J Exp Bot</ISOAbbreviation>
</Journal>
<ArticleTitle>Dynamic changes in the subcellular distribution of the tobacco ROS-producing enzyme RBOHD in response to the oomycete elicitor cryptogein.</ArticleTitle>
<Pagination><MedlinePgn>5011-22</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1093/jxb/eru265</ELocationID>
<Abstract><AbstractText>Plant NADPH oxidases, also known as respiratory burst oxidase homologues (RBOHs), have been identified as a major source of reactive oxygen species (ROS) during plant-microbe interactions. The subcellular localization of the tobacco (Nicotiana tabacum) ROS-producing enzyme RBOHD was examined in Bright Yellow-2 cells before and after elicitation with the oomycete protein cryptogein using electron and confocal microscopy. The plasma membrane (PM) localization of RBOHD was confirmed and immuno-electron microscopy on purified PM vesicles revealed its distribution in clusters. The presence of the protein fused to GFP was also seen in intracellular compartments, mainly Golgi cisternae. Cryptogein induced, within 1h, a 1.5-fold increase in RBOHD abundance at the PM and a concomitant decrease in the internal compartments. Use of cycloheximide revealed that most of the proteins targeted to the PM upon elicitation were not newly synthesized but may originate from the Golgi pool. ROS accumulation preceded RBOHD transcript- and protein-upregulation, indicating that ROS resulted from the activation of a PM-resident pool of enzymes, and that enzymes newly addressed to the PM were inactive. Taken together, the results indicate that control of RBOH abundance and subcellular localization may play a fundamental role in the mechanism of ROS production. </AbstractText>
<CopyrightInformation>© The Author 2014. Published by Oxford University Press on behalf of the Society for Experimental Biology.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Noirot</LastName>
<ForeName>Elodie</ForeName>
<Initials>E</Initials>
<AffiliationInfo><Affiliation>INRA, UMR1347 Agroécologie, ERL CNRS 6300, Plateforme DImaCell, Centre de Microscopie INRA/Université de Bourgogne, BP 86510, F-21065 Dijon Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Der</LastName>
<ForeName>Christophe</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Université de Bourgogne, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lherminier</LastName>
<ForeName>Jeannine</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>INRA, UMR1347 Agroécologie, ERL CNRS 6300, Plateforme DImaCell, Centre de Microscopie INRA/Université de Bourgogne, BP 86510, F-21065 Dijon Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Robert</LastName>
<ForeName>Franck</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>INRA, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Moricova</LastName>
<ForeName>Pavla</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>INRA, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex, France Present address: Department of Biochemistry, Faculty of Science, Palacký University in Olomouc, Šlechtitelů 11, CZ-783 71 Olomouc, Czech Republic.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kiêu</LastName>
<ForeName>Kiên</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>INRA, UR341 Mathématiques et Informatique Appliquées, F-78352 Jouy-en-Josas Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Leborgne-Castel</LastName>
<ForeName>Nathalie</ForeName>
<Initials>N</Initials>
<AffiliationInfo><Affiliation>Université de Bourgogne, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Simon-Plas</LastName>
<ForeName>Françoise</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>INRA, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bouhidel</LastName>
<ForeName>Karim</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Université de Bourgogne, UMR1347 Agroécologie, ERL CNRS 6300, BP 86510, F-21065 Dijon Cedex, France karim.bouhidel@u-bourgogne.fr.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2014</Year>
<Month>07</Month>
<Day>01</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>England</Country>
<MedlineTA>J Exp Bot</MedlineTA>
<NlmUniqueID>9882906</NlmUniqueID>
<ISSNLinking>0022-0957</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D005656">Fungal Proteins</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>EC 1.6.3.-</RegistryNumber>
<NameOfSubstance UI="D019255">NADPH Oxidases</NameOfSubstance>
</Chemical>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D002462" MajorTopicYN="N">Cell Membrane</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018613" MajorTopicYN="N">Microscopy, Confocal</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D046529" MajorTopicYN="N">Microscopy, Electron, Transmission</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D019255" MajorTopicYN="N">NADPH Oxidases</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010838" MajorTopicYN="N">Phytophthora</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D017382" MajorTopicYN="N">Reactive Oxygen Species</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060888" MajorTopicYN="N">Real-Time Polymerase Chain Reaction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">BY-2 cells</Keyword>
<Keyword MajorTopicYN="N">Nicotiana tabacum</Keyword>
<Keyword MajorTopicYN="N">cryptogein</Keyword>
<Keyword MajorTopicYN="N">protein trafficking</Keyword>
<Keyword MajorTopicYN="N">protein trafficking.</Keyword>
<Keyword MajorTopicYN="N">reactive oxygen species</Keyword>
<Keyword MajorTopicYN="N">respiratory burst oxidase homolog D (RBOHD)</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year>
<Month>7</Month>
<Day>3</Day>
<Hour>6</Hour>
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<Month>5</Month>
<Day>29</Day>
<Hour>6</Hour>
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<Reference><Citation>Plant J. 1998 May;14(3):365-70</Citation>
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</ArticleIdList>
</Reference>
</ReferenceList>
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<affiliations><list><country><li>France</li>
<li>République tchèque</li>
</country>
<region><li>Bourgogne</li>
<li>Bourgogne-Franche-Comté</li>
<li>Île-de-France</li>
</region>
<settlement><li>Dijon</li>
<li>Jouy-en-Josas</li>
</settlement>
<orgName><li>Université de Bourgogne</li>
</orgName>
</list>
<tree><country name="France"><region name="Bourgogne-Franche-Comté"><name sortKey="Noirot, Elodie" sort="Noirot, Elodie" uniqKey="Noirot E" first="Elodie" last="Noirot">Elodie Noirot</name>
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<name sortKey="Bouhidel, Karim" sort="Bouhidel, Karim" uniqKey="Bouhidel K" first="Karim" last="Bouhidel">Karim Bouhidel</name>
<name sortKey="Der, Christophe" sort="Der, Christophe" uniqKey="Der C" first="Christophe" last="Der">Christophe Der</name>
<name sortKey="Kieu, Kien" sort="Kieu, Kien" uniqKey="Kieu K" first="Kiên" last="Kiêu">Kiên Kiêu</name>
<name sortKey="Leborgne Castel, Nathalie" sort="Leborgne Castel, Nathalie" uniqKey="Leborgne Castel N" first="Nathalie" last="Leborgne-Castel">Nathalie Leborgne-Castel</name>
<name sortKey="Lherminier, Jeannine" sort="Lherminier, Jeannine" uniqKey="Lherminier J" first="Jeannine" last="Lherminier">Jeannine Lherminier</name>
<name sortKey="Robert, Franck" sort="Robert, Franck" uniqKey="Robert F" first="Franck" last="Robert">Franck Robert</name>
<name sortKey="Simon Plas, Francoise" sort="Simon Plas, Francoise" uniqKey="Simon Plas F" first="Françoise" last="Simon-Plas">Françoise Simon-Plas</name>
</country>
<country name="République tchèque"><noRegion><name sortKey="Moricova, Pavla" sort="Moricova, Pavla" uniqKey="Moricova P" first="Pavla" last="Moricova">Pavla Moricova</name>
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   |texte=   Dynamic changes in the subcellular distribution of the tobacco ROS-producing enzyme RBOHD in response to the oomycete elicitor cryptogein.
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Dynamic changes in the subcellular distribution of the tobacco ROS-producing enzyme RBOHD in response to the oomycete elicitor cryptogein.

Dynamic changes in the subcellular distribution of the tobacco ROS-producing enzyme RBOHD in response to the oomycete elicitor cryptogein.

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