Cysteine: A multifaceted amino acid involved in signaling, plant resistance and antifungal development.
Identifieur interne : 000269 ( Main/Exploration ); précédent : 000268; suivant : 000270Cysteine: A multifaceted amino acid involved in signaling, plant resistance and antifungal development.
Auteurs : Gabriel Roblin [France] ; Stéphane Octave [France] ; Mireille Faucher [France] ; Pierrette Fleurat-Lessard [France] ; Jean-Marc Berjeaud [France]Source :
- Plant physiology and biochemistry : PPB [ 1873-2690 ] ; 2018.
Descripteurs français
- KwdFr :
- Ascomycota (MeSH), Cassia (microbiologie), Cassia (physiologie), Cystéine (physiologie), Feuilles de plante (microbiologie), Feuilles de plante (métabolisme), Maladies des plantes (microbiologie), Microscopie électronique (MeSH), Mimosa (microbiologie), Mimosa (physiologie), Résistance à la maladie (physiologie), Transduction du signal (physiologie), Vitis (microbiologie), Vitis (physiologie).
- MESH :
- microbiologie : Cassia, Feuilles de plante, Maladies des plantes, Mimosa, Vitis.
- métabolisme : Feuilles de plante.
- physiologie : Cassia, Cystéine, Mimosa, Résistance à la maladie, Transduction du signal, Vitis.
- Ascomycota, Microscopie électronique.
English descriptors
- KwdEn :
- Ascomycota (MeSH), Cassia (microbiology), Cassia (physiology), Cysteine (physiology), Disease Resistance (physiology), Microscopy, Electron (MeSH), Mimosa (microbiology), Mimosa (physiology), Plant Diseases (microbiology), Plant Leaves (metabolism), Plant Leaves (microbiology), Signal Transduction (physiology), Vitis (microbiology), Vitis (physiology).
- MESH :
- chemical , physiology : Cysteine.
- metabolism : Plant Leaves.
- microbiology : Cassia, Mimosa, Plant Diseases, Plant Leaves, Vitis.
- physiology : Cassia, Disease Resistance, Mimosa, Signal Transduction, Vitis.
- Ascomycota, Microscopy, Electron.
Abstract
Early effects induced by cysteine were monitored using the model of Mimosa pudica pulvinar cells. Rapid dose-dependent membrane depolarization (within seconds) and modification of proton secretion (within minutes) were triggered at cysteine concentrations higher than 0.1 mM. These effects did not result from a modification of the plasma membrane H+-ATPase activity nor from a protonophore effect as shown by assays on plasma membrane vesicles isolated from pulvinar tissues. In a 0.5-10 mM range, cysteine inhibited the ion-driven turgor-mediated seismonastic reaction of Mimosa pudica primary pulvini and the dark-induced movement of Cassia fasciculata leaflets. At concentrations higher than 1 mM, it induced a long-lasting leaflet necrosis dependent on the concentration and treatment duration. Electron microscopy showed that cysteine induced important damage in the nucleus, mitochondria, endoplasmic reticulum and Golgi of the M. pudica motor cell. Cysteine inhibited in a concentration-dependent manner, from 0.5 to 20 mM, both the mycelial growth and the spore germination of the fungal pathogens Phaeomoniella chlamydospora and Phaeoacremonium minimum implicated in esca disease of grapevines. Using [35S] cysteine, we showed that the amino acid was absorbed following leaf spraying, translocated from leaves to other parts of grapevine cuttings and accumulated within trunks and roots. Therefore, cysteine showed relevant properties to be a candidate able to control fungal diseases either by acting as an early signal directing plant host reaction or/and by acting directly on fungal development.
DOI: 10.1016/j.plaphy.2018.05.024
PubMed: 29852365
Affiliations:
- France
- Hauts-de-France, Nouvelle-Aquitaine, Picardie, Poitou-Charentes
- Compiègne, Poitiers
- Université de Poitiers
Links toward previous steps (curation, corpus...)
Le document en format XML
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Ascomycota (MeSH)</term>
<term>Cassia (microbiology)</term>
<term>Cassia (physiology)</term>
<term>Cysteine (physiology)</term>
<term>Disease Resistance (physiology)</term>
<term>Microscopy, Electron (MeSH)</term>
<term>Mimosa (microbiology)</term>
<term>Mimosa (physiology)</term>
<term>Plant Diseases (microbiology)</term>
<term>Plant Leaves (metabolism)</term>
<term>Plant Leaves (microbiology)</term>
<term>Signal Transduction (physiology)</term>
<term>Vitis (microbiology)</term>
<term>Vitis (physiology)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Ascomycota (MeSH)</term>
<term>Cassia (microbiologie)</term>
<term>Cassia (physiologie)</term>
<term>Cystéine (physiologie)</term>
<term>Feuilles de plante (microbiologie)</term>
<term>Feuilles de plante (métabolisme)</term>
<term>Maladies des plantes (microbiologie)</term>
<term>Microscopie électronique (MeSH)</term>
<term>Mimosa (microbiologie)</term>
<term>Mimosa (physiologie)</term>
<term>Résistance à la maladie (physiologie)</term>
<term>Transduction du signal (physiologie)</term>
<term>Vitis (microbiologie)</term>
<term>Vitis (physiologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Cysteine</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plant Leaves</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Cassia</term>
<term>Feuilles de plante</term>
<term>Maladies des plantes</term>
<term>Mimosa</term>
<term>Vitis</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Cassia</term>
<term>Mimosa</term>
<term>Plant Diseases</term>
<term>Plant Leaves</term>
<term>Vitis</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Feuilles de plante</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cassia</term>
<term>Cystéine</term>
<term>Mimosa</term>
<term>Résistance à la maladie</term>
<term>Transduction du signal</term>
<term>Vitis</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cassia</term>
<term>Disease Resistance</term>
<term>Mimosa</term>
<term>Signal Transduction</term>
<term>Vitis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Ascomycota</term>
<term>Microscopy, Electron</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Ascomycota</term>
<term>Microscopie électronique</term>
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<front><div type="abstract" xml:lang="en">Early effects induced by cysteine were monitored using the model of Mimosa pudica pulvinar cells. Rapid dose-dependent membrane depolarization (within seconds) and modification of proton secretion (within minutes) were triggered at cysteine concentrations higher than 0.1 mM. These effects did not result from a modification of the plasma membrane H<sup>+</sup>
-ATPase activity nor from a protonophore effect as shown by assays on plasma membrane vesicles isolated from pulvinar tissues. In a 0.5-10 mM range, cysteine inhibited the ion-driven turgor-mediated seismonastic reaction of Mimosa pudica primary pulvini and the dark-induced movement of Cassia fasciculata leaflets. At concentrations higher than 1 mM, it induced a long-lasting leaflet necrosis dependent on the concentration and treatment duration. Electron microscopy showed that cysteine induced important damage in the nucleus, mitochondria, endoplasmic reticulum and Golgi of the M. pudica motor cell. Cysteine inhibited in a concentration-dependent manner, from 0.5 to 20 mM, both the mycelial growth and the spore germination of the fungal pathogens Phaeomoniella chlamydospora and Phaeoacremonium minimum implicated in esca disease of grapevines. Using [<sup>35</sup>
S] cysteine, we showed that the amino acid was absorbed following leaf spraying, translocated from leaves to other parts of grapevine cuttings and accumulated within trunks and roots. Therefore, cysteine showed relevant properties to be a candidate able to control fungal diseases either by acting as an early signal directing plant host reaction or/and by acting directly on fungal development.</div>
</front>
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<ArticleTitle>Cysteine: A multifaceted amino acid involved in signaling, plant resistance and antifungal development.</ArticleTitle>
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<Abstract><AbstractText>Early effects induced by cysteine were monitored using the model of Mimosa pudica pulvinar cells. Rapid dose-dependent membrane depolarization (within seconds) and modification of proton secretion (within minutes) were triggered at cysteine concentrations higher than 0.1 mM. These effects did not result from a modification of the plasma membrane H<sup>+</sup>
-ATPase activity nor from a protonophore effect as shown by assays on plasma membrane vesicles isolated from pulvinar tissues. In a 0.5-10 mM range, cysteine inhibited the ion-driven turgor-mediated seismonastic reaction of Mimosa pudica primary pulvini and the dark-induced movement of Cassia fasciculata leaflets. At concentrations higher than 1 mM, it induced a long-lasting leaflet necrosis dependent on the concentration and treatment duration. Electron microscopy showed that cysteine induced important damage in the nucleus, mitochondria, endoplasmic reticulum and Golgi of the M. pudica motor cell. Cysteine inhibited in a concentration-dependent manner, from 0.5 to 20 mM, both the mycelial growth and the spore germination of the fungal pathogens Phaeomoniella chlamydospora and Phaeoacremonium minimum implicated in esca disease of grapevines. Using [<sup>35</sup>
S] cysteine, we showed that the amino acid was absorbed following leaf spraying, translocated from leaves to other parts of grapevine cuttings and accumulated within trunks and roots. Therefore, cysteine showed relevant properties to be a candidate able to control fungal diseases either by acting as an early signal directing plant host reaction or/and by acting directly on fungal development.</AbstractText>
<CopyrightInformation>Copyright © 2018 Elsevier Masson SAS. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Roblin</LastName>
<ForeName>Gabriel</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Université de Poitiers, Ecologie & Biologie des Interactions, UMR CNRS 7267, 1 rue Georges Bonnet, TSA51106, 86073 Poitiers cedex 9, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Octave</LastName>
<ForeName>Stéphane</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Université de Poitiers, Ecologie & Biologie des Interactions, UMR CNRS 7267, 1 rue Georges Bonnet, TSA51106, 86073 Poitiers cedex 9, France; Current address: Sorbonne Universités, Université de Technologie de Compiègne, UMR CNRS 7025, Génie Enzymatique et Cellulaire, Rue du Docteur Schweitzer CS 60319, 60203 Compiègne Cedex, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Faucher</LastName>
<ForeName>Mireille</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Université de Poitiers, Ecologie & Biologie des Interactions, UMR CNRS 7267, 1 rue Georges Bonnet, TSA51106, 86073 Poitiers cedex 9, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Fleurat-Lessard</LastName>
<ForeName>Pierrette</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Université de Poitiers, Ecologie & Biologie des Interactions, UMR CNRS 7267, 1 rue Georges Bonnet, TSA51106, 86073 Poitiers cedex 9, France.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Berjeaud</LastName>
<ForeName>Jean-Marc</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>Université de Poitiers, Ecologie & Biologie des Interactions, UMR CNRS 7267, 1 rue Georges Bonnet, TSA51106, 86073 Poitiers cedex 9, France. Electronic address: jean-marc.berjeaud@univ-poitiers.fr.</Affiliation>
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</Author>
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<Language>eng</Language>
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<Month>05</Month>
<Day>23</Day>
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<MedlineJournalInfo><Country>France</Country>
<MedlineTA>Plant Physiol Biochem</MedlineTA>
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<ChemicalList><Chemical><RegistryNumber>K848JZ4886</RegistryNumber>
<NameOfSubstance UI="D003545">Cysteine</NameOfSubstance>
</Chemical>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D001203" MajorTopicYN="N">Ascomycota</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002366" MajorTopicYN="N">Cassia</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003545" MajorTopicYN="N">Cysteine</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D060467" MajorTopicYN="N">Disease Resistance</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D031298" MajorTopicYN="N">Mimosa</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018515" MajorTopicYN="N">Plant Leaves</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="Y">Signal Transduction</DescriptorName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D027843" MajorTopicYN="N">Vitis</DescriptorName>
<QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName>
<QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName>
</MeshHeading>
</MeshHeadingList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year>
<Month>03</Month>
<Day>20</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2018</Year>
<Month>05</Month>
<Day>04</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2018</Year>
<Month>05</Month>
<Day>22</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2018</Year>
<Month>6</Month>
<Day>1</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="medline"><Year>2019</Year>
<Month>2</Month>
<Day>13</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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<PubMedPubDate PubStatus="entrez"><Year>2018</Year>
<Month>6</Month>
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</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">29852365</ArticleId>
<ArticleId IdType="pii">S0981-9428(18)30241-9</ArticleId>
<ArticleId IdType="doi">10.1016/j.plaphy.2018.05.024</ArticleId>
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</PubmedData>
</pubmed>
<affiliations><list><country><li>France</li>
</country>
<region><li>Hauts-de-France</li>
<li>Nouvelle-Aquitaine</li>
<li>Picardie</li>
<li>Poitou-Charentes</li>
</region>
<settlement><li>Compiègne</li>
<li>Poitiers</li>
</settlement>
<orgName><li>Université de Poitiers</li>
</orgName>
</list>
<tree><country name="France"><region name="Nouvelle-Aquitaine"><name sortKey="Roblin, Gabriel" sort="Roblin, Gabriel" uniqKey="Roblin G" first="Gabriel" last="Roblin">Gabriel Roblin</name>
</region>
<name sortKey="Berjeaud, Jean Marc" sort="Berjeaud, Jean Marc" uniqKey="Berjeaud J" first="Jean-Marc" last="Berjeaud">Jean-Marc Berjeaud</name>
<name sortKey="Faucher, Mireille" sort="Faucher, Mireille" uniqKey="Faucher M" first="Mireille" last="Faucher">Mireille Faucher</name>
<name sortKey="Fleurat Lessard, Pierrette" sort="Fleurat Lessard, Pierrette" uniqKey="Fleurat Lessard P" first="Pierrette" last="Fleurat-Lessard">Pierrette Fleurat-Lessard</name>
<name sortKey="Octave, Stephane" sort="Octave, Stephane" uniqKey="Octave S" first="Stéphane" last="Octave">Stéphane Octave</name>
</country>
</tree>
</affiliations>
</record>
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