A role for S-nitrosylation of the SUMO-conjugating enzyme SCE1 in plant immunity.
S-nitrosylation
immunity
nitric oxide
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
20 08 2019
20 08 2019
Historique:
pubmed:
3
8
2019
medline:
24
3
2020
entrez:
3
8
2019
Statut:
ppublish
Résumé
SUMOylation, the covalent attachment of the small ubiquitin-like modifier (SUMO) to target proteins, is emerging as a key modulator of eukaryotic immune function. In plants, a SUMO1/2-dependent process has been proposed to control the deployment of host defense responses. The molecular mechanism underpinning this activity remains to be determined, however. Here we show that increasing nitric oxide levels following pathogen recognition promote S-nitrosylation of the
Identifiants
pubmed: 31371496
pii: 1900052116
doi: 10.1073/pnas.1900052116
pmc: PMC6708345
doi:
Substances chimiques
Arabidopsis Proteins
0
SUM2 protein, Arabidopsis
0
Nitric Oxide
31C4KY9ESH
Ubiquitin-Conjugating Enzymes
EC 2.3.2.23
At1g09730 protein, Arabidopsis
EC 3.4.22.-
Cysteine Endopeptidases
EC 3.4.22.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
17090-17095Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/H000984/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/DO11809/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/F017073/1
Pays : United Kingdom
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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