Recent Advances in the Regulation of Plant Immunity by S-Nitrosylation.
Identifieur interne : 000067 ( Main/Exploration ); précédent : 000066; suivant : 000068Recent Advances in the Regulation of Plant Immunity by S-Nitrosylation.
Auteurs : Jibril Lubega [Royaume-Uni] ; Saima Umbreen [Royaume-Uni] ; Gary J. Loake [Royaume-Uni]Source :
- Journal of experimental botany [ 1460-2431 ] ; 2020.
Abstract
S-nitrosylation, the addition of a nitric oxide (NO) moiety to a reactive protein cysteine (Cys) thiol, to form a protein S-nitrosothiol (SNO), is emerging as a key regulatory post-translational modification (PTM) to control the plant immune response. NO also S-nitrosylates the antioxidant tripeptide, glutathione (GSH), to form S-nitrosoglutathione (GSNO), both a storage reservoir of NO bioactivity and a natural NO donor. GSNO and by extension, S-nitrosylation, is controlled by GSNO reductase1 (GSNOR1). The emerging data suggests that GSNOR1 itself is a target of NO-mediated S-nitrosylation, which subsequently controls its selective autophagy, regulating cellular protein SNO levels. Recent findings also suggest that S-nitrosylation may be deployed by pathogen-challenged host cells to counteract the effect of delivered microbial effector proteins, that promote pathogenesis and by the pathogens themselves to augment virulence. Significantly, it also appears that S-nitrosylation may regulate plant immune functions by controlling SUMOylation, a peptide-based PTM. In this context, global SUMOylation is regulated by S-nitrosylation of SUMO Conjugating Enzyme 1 (SCE1) at Cys 139. This redox-based PTM has also been shown to control the function of a key zinc finger transcriptional regulator during the establishment of plant immunity. Here, we provide an update of these recent advances.
DOI: 10.1093/jxb/eraa454
PubMed: 33005916
Affiliations:
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Loake</name><affiliation wicri:level="4"><nlm:affiliation>Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh</wicri:regionArea><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName><orgName type="university">Université d'Édimbourg</orgName></affiliation><affiliation wicri:level="4"><nlm:affiliation>Centre for Synthetic and Systems Biology, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Centre for Synthetic and Systems Biology, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh</wicri:regionArea><placeName><settlement type="city">Édimbourg</settlement><region type="country">Écosse</region></placeName><orgName type="university">Université d'Édimbourg</orgName></affiliation></author></analytic><series><title level="j">Journal of experimental botany</title><idno type="eISSN">1460-2431</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">S-nitrosylation, the addition of a nitric oxide (NO) moiety to a reactive protein cysteine (Cys) thiol, to form a protein S-nitrosothiol (SNO), is emerging as a key regulatory post-translational modification (PTM) to control the plant immune response. NO also S-nitrosylates the antioxidant tripeptide, glutathione (GSH), to form S-nitrosoglutathione (GSNO), both a storage reservoir of NO bioactivity and a natural NO donor. GSNO and by extension, S-nitrosylation, is controlled by GSNO reductase1 (GSNOR1). The emerging data suggests that GSNOR1 itself is a target of NO-mediated S-nitrosylation, which subsequently controls its selective autophagy, regulating cellular protein SNO levels. Recent findings also suggest that S-nitrosylation may be deployed by pathogen-challenged host cells to counteract the effect of delivered microbial effector proteins, that promote pathogenesis and by the pathogens themselves to augment virulence. Significantly, it also appears that S-nitrosylation may regulate plant immune functions by controlling SUMOylation, a peptide-based PTM. In this context, global SUMOylation is regulated by S-nitrosylation of SUMO Conjugating Enzyme 1 (SCE1) at Cys 139. This redox-based PTM has also been shown to control the function of a key zinc finger transcriptional regulator during the establishment of plant immunity. Here, we provide an update of these recent advances.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33005916</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2431</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of experimental botany</Title><ISOAbbreviation>J Exp Bot</ISOAbbreviation></Journal><ArticleTitle>Recent Advances in the Regulation of Plant Immunity by S-Nitrosylation.</ArticleTitle><ELocationID EIdType="pii" ValidYN="Y">eraa454</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1093/jxb/eraa454</ELocationID><Abstract><AbstractText>S-nitrosylation, the addition of a nitric oxide (NO) moiety to a reactive protein cysteine (Cys) thiol, to form a protein S-nitrosothiol (SNO), is emerging as a key regulatory post-translational modification (PTM) to control the plant immune response. NO also S-nitrosylates the antioxidant tripeptide, glutathione (GSH), to form S-nitrosoglutathione (GSNO), both a storage reservoir of NO bioactivity and a natural NO donor. GSNO and by extension, S-nitrosylation, is controlled by GSNO reductase1 (GSNOR1). The emerging data suggests that GSNOR1 itself is a target of NO-mediated S-nitrosylation, which subsequently controls its selective autophagy, regulating cellular protein SNO levels. Recent findings also suggest that S-nitrosylation may be deployed by pathogen-challenged host cells to counteract the effect of delivered microbial effector proteins, that promote pathogenesis and by the pathogens themselves to augment virulence. Significantly, it also appears that S-nitrosylation may regulate plant immune functions by controlling SUMOylation, a peptide-based PTM. In this context, global SUMOylation is regulated by S-nitrosylation of SUMO Conjugating Enzyme 1 (SCE1) at Cys 139. This redox-based PTM has also been shown to control the function of a key zinc finger transcriptional regulator during the establishment of plant immunity. Here, we provide an update of these recent advances.</AbstractText><CopyrightInformation>© The Author(s) 2020. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For permissions, please email: journals.permissions@oup.com.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lubega</LastName><ForeName>Jibril</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Umbreen</LastName><ForeName>Saima</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Loake</LastName><ForeName>Gary J</ForeName><Initials>GJ</Initials><AffiliationInfo><Affiliation>Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh, UK.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Centre for Synthetic and Systems Biology, School of Biological Sciences, University of Edinburgh, The King's Buildings, Edinburgh, UK.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>10</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Exp Bot</MedlineTA><NlmUniqueID>9882906</NlmUniqueID><ISSNLinking>0022-0957</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">S-nitrosylation</Keyword><Keyword MajorTopicYN="N">SUMOylation</Keyword><Keyword MajorTopicYN="N">Zinc finger proteins</Keyword><Keyword MajorTopicYN="N">autophagy</Keyword><Keyword MajorTopicYN="N">effector</Keyword><Keyword MajorTopicYN="N">nitric oxide</Keyword><Keyword MajorTopicYN="N">plant immunity</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>06</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>10</Month><Day>2</Day><Hour>5</Hour><Minute>47</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>10</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33005916</ArticleId><ArticleId IdType="pii">5917134</ArticleId><ArticleId IdType="doi">10.1093/jxb/eraa454</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Écosse</li></region><settlement><li>Édimbourg</li></settlement><orgName><li>Université d'Édimbourg</li></orgName></list><tree><country name="Royaume-Uni"><region name="Écosse"><name sortKey="Lubega, Jibril" sort="Lubega, Jibril" uniqKey="Lubega J" first="Jibril" last="Lubega">Jibril Lubega</name></region><name sortKey="Loake, Gary J" sort="Loake, Gary J" uniqKey="Loake G" first="Gary J" last="Loake">Gary J. Loake</name><name sortKey="Loake, Gary J" sort="Loake, Gary J" uniqKey="Loake G" first="Gary J" last="Loake">Gary J. Loake</name><name sortKey="Umbreen, Saima" sort="Umbreen, Saima" uniqKey="Umbreen S" first="Saima" last="Umbreen">Saima Umbreen</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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