Phosphorylation of the Pseudomonas Effector AvrPtoB by Arabidopsis SnRK2.8 Is Required for Bacterial Virulence.
Arabidopsis
AvrPtoB
Pseudomonas syringae
SnRK2.8
effector
kinase
Journal
Molecular plant
ISSN: 1752-9867
Titre abrégé: Mol Plant
Pays: England
ID NLM: 101465514
Informations de publication
Date de publication:
05 10 2020
05 10 2020
Historique:
received:
21
03
2020
revised:
20
08
2020
accepted:
30
08
2020
pubmed:
6
9
2020
medline:
22
6
2021
entrez:
5
9
2020
Statut:
ppublish
Résumé
A critical component controlling bacterial virulence is the delivery of pathogen effectors into plant cells during infection. Effectors alter host metabolism and immunity for the benefit of pathogens. Multiple effectors are phosphorylated by host kinases, and this posttranslational modification is important for their activity. We sought to identify host kinases involved in effector phosphorylation. Multiple phosphorylated effector residues matched the proposed consensus motif for the plant calcium-dependent protein kinase (CDPK) and Snf1-related kinase (SnRK) superfamily. The conserved Pseudomonas effector AvrPtoB acts as an E3 ubiquitin ligase and promotes bacterial virulence. In this study, we identified a member of the Arabidopsis SnRK family, SnRK2.8, which interacts with AvrPtoB in yeast and in planta. We showed that SnRK2.8 was required for AvrPtoB virulence functions, including facilitating bacterial colonization, suppression of callose deposition, and targeting the plant defense regulator NPR1 and analyses receptor FLS2. Mass spectrometry analysis revealed that AvrPtoB phosphorylation occurs at multiple serine residues in planta, with S258 phosphorylation significantly reduced in the snrk2.8 knockout. AvrPtoB phospho-null mutants exhibited compromised virulence functions and were unable to suppress NPR1 accumulation, FLS2 accumulation, or inhibit FLS2-BAK1 complex formation upon flagellin perception. Taken together, these data identify a conserved plant kinase utilized by a pathogen effector to promote disease.
Identifiants
pubmed: 32889173
pii: S1674-2052(20)30295-1
doi: 10.1016/j.molp.2020.08.018
pmc: PMC7808569
mid: NIHMS1627021
pii:
doi:
Substances chimiques
Arabidopsis Proteins
0
Bacterial Proteins
0
SnRK2 protein, Arabidopsis
0
avrPto protein, Pseudomonas syringae
0
Ubiquitin-Protein Ligases
EC 2.3.2.27
Protein Kinases
EC 2.7.-
FLS2 protein, Arabidopsis
EC 2.7.1.-
SNF1-related protein kinases
EC 2.7.1.-
calcium-dependent protein kinase
EC 2.7.1.-
Protein Serine-Threonine Kinases
EC 2.7.11.1
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
1513-1522Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM092772
Pays : United States
Organisme : NIGMS NIH HHS
ID : R35 GM136402
Pays : United States
Organisme : NIH HHS
ID : S10 OD021801
Pays : United States
Informations de copyright
Copyright © 2020 The Author. Published by Elsevier Inc. All rights reserved.
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