Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco cells.
Identifieur interne : 001482 ( Main/Exploration ); précédent : 001481; suivant : 001483Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco cells.
Auteurs : Jéremy Astier [France] ; Angélique Besson-Bard ; Olivier Lamotte ; Jean Bertoldo ; Stéphane Bourque ; Hernán Terenzi ; David WendehenneSource :
- The Biochemical journal [ 1470-8728 ] ; 2012.
Descripteurs français
- KwdFr :
- Adenosine triphosphatases (antagonistes et inhibiteurs), Adenosine triphosphatases (composition chimique), Adenosine triphosphatases (métabolisme), Conformation des protéines (effets des médicaments et des substances chimiques), Données de séquences moléculaires (MeSH), Modèles moléculaires (MeSH), Monoxyde d'azote (pharmacologie), Protéine contenant la valosine (MeSH), Protéines du cycle cellulaire (antagonistes et inhibiteurs), Protéines du cycle cellulaire (composition chimique), Protéines du cycle cellulaire (métabolisme), Protéines fongiques (pharmacologie), Protéines végétales (effets des médicaments et des substances chimiques), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Tabac (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Adenosine triphosphatases, Protéines du cycle cellulaire.
- composition chimique : Adenosine triphosphatases, Protéines du cycle cellulaire.
- effets des médicaments et des substances chimiques : Conformation des protéines, Protéines végétales.
- métabolisme : Adenosine triphosphatases, Protéines du cycle cellulaire, Tabac.
- pharmacologie : Monoxyde d'azote, Protéines fongiques.
- Données de séquences moléculaires, Modèles moléculaires, Protéine contenant la valosine, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Adenosine Triphosphatases (antagonists & inhibitors), Adenosine Triphosphatases (chemistry), Adenosine Triphosphatases (metabolism), Amino Acid Sequence (MeSH), Cell Cycle Proteins (antagonists & inhibitors), Cell Cycle Proteins (chemistry), Cell Cycle Proteins (metabolism), Fungal Proteins (pharmacology), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nitric Oxide (pharmacology), Plant Proteins (drug effects), Protein Conformation (drug effects), Protein Structure, Tertiary (MeSH), Tobacco (metabolism), Valosin Containing Protein (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Adenosine Triphosphatases, Cell Cycle Proteins.
- chemical , chemistry : Adenosine Triphosphatases, Cell Cycle Proteins.
- chemical , drug effects : Plant Proteins.
- chemical , metabolism : Adenosine Triphosphatases, Cell Cycle Proteins.
- chemical , pharmacology : Fungal Proteins, Nitric Oxide.
- drug effects : Protein Conformation.
- metabolism : Tobacco.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Protein Structure, Tertiary, Valosin Containing Protein.
Abstract
NO has important physiological functions in plants, including the adaptative response to pathogen attack. We previously demonstrated that cryptogein, an elicitor of defence reaction produced by the oomycete Phytophthora cryptogea, triggers NO synthesis in tobacco. To decipher the role of NO in tobacco cells elicited by cryptogein, in the present study we performed a proteomic approach in order to identify proteins undergoing S-nitrosylation. We provided evidence that cryptogein induced the S-nitrosylation of several proteins and identified 11 candidates, including CDC48 (cell division cycle 48), a member of the AAA+ ATPase (ATPase associated with various cellular activities) family. In vitro, NtCDC48 (Nicotiana tabacum CDC48) was shown to be poly-S-nitrosylated by NO donors and we could identify Cys(110), Cys(526) and Cys(664) as a targets for S-nitrosylation. Cys(526) is located in the Walker A motif of the D2 domain, that is involved in ATP binding and was previously reported to be regulated by oxidative modification in Drosophila. We investigated the consequence of NtCDC48 S-nitrosylation and found that NO abolished NtCDC48 ATPase activity and induced slight conformation changes in the vicinity of Cys(526). Similarly, substitution of Cys(526) by an alanine residue had an impact on NtCDC48 activity. More generally, the present study identified CDC48 as a new candidate for S-nitrosylation in plants facing biotic stress and further supports the importance of Cys(526) in the regulation of CDC48 by oxidative/nitrosative agents.
DOI: 10.1042/BJ20120257
PubMed: 22835150
Affiliations:
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Agroécologie AgroSup Dijon/INRA/Université de Bourgogne, Pôle Mécanisme et Gestion des Interactions Plantes-microorganismes - ERL CNRS 6300, Dijon, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>UMR 1347 Agroécologie AgroSup Dijon/INRA/Université de Bourgogne, Pôle Mécanisme et Gestion des Interactions Plantes-microorganismes - ERL CNRS 6300, Dijon</wicri:regionArea><placeName><region type="region">Bourgogne-Franche-Comté</region><region type="old region">Bourgogne</region><settlement type="city">Dijon</settlement></placeName><orgName type="university">Université de Bourgogne</orgName></affiliation></author><author><name sortKey="Besson Bard, Angelique" sort="Besson Bard, Angelique" uniqKey="Besson Bard A" first="Angélique" last="Besson-Bard">Angélique Besson-Bard</name></author><author><name sortKey="Lamotte, Olivier" sort="Lamotte, Olivier" uniqKey="Lamotte O" first="Olivier" last="Lamotte">Olivier Lamotte</name></author><author><name sortKey="Bertoldo, Jean" sort="Bertoldo, Jean" uniqKey="Bertoldo J" first="Jean" last="Bertoldo">Jean Bertoldo</name></author><author><name sortKey="Bourque, Stephane" sort="Bourque, Stephane" uniqKey="Bourque S" first="Stéphane" last="Bourque">Stéphane Bourque</name></author><author><name sortKey="Terenzi, Hernan" sort="Terenzi, Hernan" uniqKey="Terenzi H" first="Hernán" last="Terenzi">Hernán Terenzi</name></author><author><name sortKey="Wendehenne, David" sort="Wendehenne, David" uniqKey="Wendehenne D" first="David" last="Wendehenne">David Wendehenne</name></author></analytic><series><title level="j">The Biochemical journal</title><idno type="eISSN">1470-8728</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (antagonists & inhibitors)</term><term>Adenosine Triphosphatases (chemistry)</term><term>Adenosine Triphosphatases (metabolism)</term><term>Amino Acid Sequence (MeSH)</term><term>Cell Cycle Proteins (antagonists & inhibitors)</term><term>Cell Cycle Proteins (chemistry)</term><term>Cell Cycle Proteins (metabolism)</term><term>Fungal Proteins (pharmacology)</term><term>Models, Molecular (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Nitric Oxide (pharmacology)</term><term>Plant Proteins (drug effects)</term><term>Protein Conformation (drug effects)</term><term>Protein Structure, Tertiary (MeSH)</term><term>Tobacco (metabolism)</term><term>Valosin Containing Protein (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adenosine triphosphatases (antagonistes et inhibiteurs)</term><term>Adenosine triphosphatases (composition chimique)</term><term>Adenosine triphosphatases (métabolisme)</term><term>Conformation des protéines (effets des médicaments et des substances chimiques)</term><term>Données de séquences moléculaires (MeSH)</term><term>Modèles moléculaires (MeSH)</term><term>Monoxyde d'azote (pharmacologie)</term><term>Protéine contenant la valosine (MeSH)</term><term>Protéines du cycle cellulaire (antagonistes et inhibiteurs)</term><term>Protéines du cycle cellulaire (composition chimique)</term><term>Protéines du cycle cellulaire (métabolisme)</term><term>Protéines fongiques (pharmacologie)</term><term>Protéines végétales (effets des médicaments et des substances chimiques)</term><term>Structure tertiaire des protéines (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term><term>Tabac (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Cell Cycle Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Cell Cycle Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Cell Cycle Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Fungal Proteins</term><term>Nitric Oxide</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Protéines du cycle cellulaire</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Protéines du cycle cellulaire</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Protein Conformation</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Conformation des protéines</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Protéines du cycle cellulaire</term><term>Tabac</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Monoxyde d'azote</term><term>Protéines fongiques</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Valosin Containing Protein</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Données de séquences moléculaires</term><term>Modèles moléculaires</term><term>Protéine contenant la valosine</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">NO has important physiological functions in plants, including the adaptative response to pathogen attack. We previously demonstrated that cryptogein, an elicitor of defence reaction produced by the oomycete Phytophthora cryptogea, triggers NO synthesis in tobacco. To decipher the role of NO in tobacco cells elicited by cryptogein, in the present study we performed a proteomic approach in order to identify proteins undergoing S-nitrosylation. We provided evidence that cryptogein induced the S-nitrosylation of several proteins and identified 11 candidates, including CDC48 (cell division cycle 48), a member of the AAA+ ATPase (ATPase associated with various cellular activities) family. In vitro, NtCDC48 (Nicotiana tabacum CDC48) was shown to be poly-S-nitrosylated by NO donors and we could identify Cys(110), Cys(526) and Cys(664) as a targets for S-nitrosylation. Cys(526) is located in the Walker A motif of the D2 domain, that is involved in ATP binding and was previously reported to be regulated by oxidative modification in Drosophila. We investigated the consequence of NtCDC48 S-nitrosylation and found that NO abolished NtCDC48 ATPase activity and induced slight conformation changes in the vicinity of Cys(526). Similarly, substitution of Cys(526) by an alanine residue had an impact on NtCDC48 activity. More generally, the present study identified CDC48 as a new candidate for S-nitrosylation in plants facing biotic stress and further supports the importance of Cys(526) in the regulation of CDC48 by oxidative/nitrosative agents.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22835150</PMID><DateCompleted><Year>2012</Year><Month>12</Month><Day>07</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1470-8728</ISSN><JournalIssue CitedMedium="Internet"><Volume>447</Volume><Issue>2</Issue><PubDate><Year>2012</Year><Month>Oct</Month><Day>15</Day></PubDate></JournalIssue><Title>The Biochemical journal</Title><ISOAbbreviation>Biochem J</ISOAbbreviation></Journal><ArticleTitle>Nitric oxide inhibits the ATPase activity of the chaperone-like AAA+ ATPase CDC48, a target for S-nitrosylation in cryptogein signalling in tobacco cells.</ArticleTitle><Pagination><MedlinePgn>249-60</MedlinePgn></Pagination><Abstract><AbstractText>NO has important physiological functions in plants, including the adaptative response to pathogen attack. We previously demonstrated that cryptogein, an elicitor of defence reaction produced by the oomycete Phytophthora cryptogea, triggers NO synthesis in tobacco. To decipher the role of NO in tobacco cells elicited by cryptogein, in the present study we performed a proteomic approach in order to identify proteins undergoing S-nitrosylation. We provided evidence that cryptogein induced the S-nitrosylation of several proteins and identified 11 candidates, including CDC48 (cell division cycle 48), a member of the AAA+ ATPase (ATPase associated with various cellular activities) family. In vitro, NtCDC48 (Nicotiana tabacum CDC48) was shown to be poly-S-nitrosylated by NO donors and we could identify Cys(110), Cys(526) and Cys(664) as a targets for S-nitrosylation. Cys(526) is located in the Walker A motif of the D2 domain, that is involved in ATP binding and was previously reported to be regulated by oxidative modification in Drosophila. We investigated the consequence of NtCDC48 S-nitrosylation and found that NO abolished NtCDC48 ATPase activity and induced slight conformation changes in the vicinity of Cys(526). Similarly, substitution of Cys(526) by an alanine residue had an impact on NtCDC48 activity. More generally, the present study identified CDC48 as a new candidate for S-nitrosylation in plants facing biotic stress and further supports the importance of Cys(526) in the regulation of CDC48 by oxidative/nitrosative agents.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Astier</LastName><ForeName>Jéremy</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>UMR 1347 Agroécologie AgroSup Dijon/INRA/Université de Bourgogne, Pôle Mécanisme et Gestion des Interactions Plantes-microorganismes - ERL CNRS 6300, Dijon, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Besson-Bard</LastName><ForeName>Angélique</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Lamotte</LastName><ForeName>Olivier</ForeName><Initials>O</Initials></Author><Author ValidYN="Y"><LastName>Bertoldo</LastName><ForeName>Jean</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Bourque</LastName><ForeName>Stéphane</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Terenzi</LastName><ForeName>Hernán</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Wendehenne</LastName><ForeName>David</ForeName><Initials>D</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>Biochem J</MedlineTA><NlmUniqueID>2984726R</NlmUniqueID><ISSNLinking>0264-6021</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018797">Cell Cycle Proteins</NameOfSubstance></Chemical><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="C061032">cryptogein protein, Phytophthora cryptogea</NameOfSubstance></Chemical><Chemical><RegistryNumber>31C4KY9ESH</RegistryNumber><NameOfSubstance UI="D009569">Nitric Oxide</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.4.6</RegistryNumber><NameOfSubstance UI="D000074405">Valosin Containing Protein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018797" MajorTopicYN="N">Cell Cycle Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009569" MajorTopicYN="N">Nitric Oxide</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014026" MajorTopicYN="N">Tobacco</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000074405" MajorTopicYN="N">Valosin Containing Protein</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>7</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>7</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>12</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22835150</ArticleId><ArticleId IdType="pii">BJ20120257</ArticleId><ArticleId IdType="doi">10.1042/BJ20120257</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>France</li></country><region><li>Bourgogne</li><li>Bourgogne-Franche-Comté</li></region><settlement><li>Dijon</li></settlement><orgName><li>Université de Bourgogne</li></orgName></list><tree><noCountry><name sortKey="Bertoldo, Jean" sort="Bertoldo, Jean" uniqKey="Bertoldo J" first="Jean" last="Bertoldo">Jean Bertoldo</name><name sortKey="Besson Bard, Angelique" sort="Besson Bard, Angelique" uniqKey="Besson Bard A" first="Angélique" last="Besson-Bard">Angélique Besson-Bard</name><name sortKey="Bourque, Stephane" sort="Bourque, Stephane" uniqKey="Bourque S" first="Stéphane" last="Bourque">Stéphane Bourque</name><name sortKey="Lamotte, Olivier" sort="Lamotte, Olivier" uniqKey="Lamotte O" first="Olivier" last="Lamotte">Olivier Lamotte</name><name sortKey="Terenzi, Hernan" sort="Terenzi, Hernan" uniqKey="Terenzi H" first="Hernán" last="Terenzi">Hernán Terenzi</name><name sortKey="Wendehenne, David" sort="Wendehenne, David" uniqKey="Wendehenne D" first="David" last="Wendehenne">David Wendehenne</name></noCountry><country name="France"><region name="Bourgogne-Franche-Comté"><name sortKey="Astier, Jeremy" sort="Astier, Jeremy" uniqKey="Astier J" first="Jéremy" last="Astier">Jéremy Astier</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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