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Cell. 2015 May 21;161(5):1074-1088. doi: 10.1016/j.cell.2015.04.025.

A receptor pair with an integrated decoy converts pathogen disabling of transcription factors to immunity.

Author information

1
INRA, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR441, Castanet-Tolosan 31326, France; CNRS, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR2594, Castanet-Tolosan 31326, France; Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, Köln 50829, Germany.
2
INRA, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR441, Castanet-Tolosan 31326, France; CNRS, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR2594, Castanet-Tolosan 31326, France.
3
Institut Fédératif de Recherche 3450, Plateforme Imagerie, Pôle de Biotechnologie Végétale, Castanet-Tolosan 31326, France.
4
Laboratoire de Recherche en Sciences Végétales, Université de Toulouse, UPS, UMR 5546, BP 42617 Auzeville, Castanet-Tolosan 31326, France; CNRS, UMR 5546, BP 42617, Castanet-Tolosan 31326, France.
5
Université Grenoble Alpes, iRTSV-BGE, Grenoble 38000, France; CEA, iRTSV-BGE, Grenoble 38000, France; INSERM, BGE, Grenoble 38000, France.
6
Defense in Plant-Pathogen Interactions, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
7
Department of Plant-Microbe Interactions, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, Köln 50829, Germany.
8
INRA, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR441, Castanet-Tolosan 31326, France; CNRS, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR2594, Castanet-Tolosan 31326, France. Electronic address: laurent.deslandes@toulouse.inra.fr.

Abstract

Microbial pathogens infect host cells by delivering virulence factors (effectors) that interfere with defenses. In plants, intracellular nucleotide-binding/leucine-rich repeat receptors (NLRs) detect specific effector interference and trigger immunity by an unknown mechanism. The Arabidopsis-interacting NLR pair, RRS1-R with RPS4, confers resistance to different pathogens, including Ralstonia solanacearum bacteria expressing the acetyltransferase effector PopP2. We show that PopP2 directly acetylates a key lysine within an additional C-terminal WRKY transcription factor domain of RRS1-R that binds DNA. This disrupts RRS1-R DNA association and activates RPS4-dependent immunity. PopP2 uses the same lysine acetylation strategy to target multiple defense-promoting WRKY transcription factors, causing loss of WRKY-DNA binding and transactivating functions needed for defense gene expression and disease resistance. Thus, RRS1-R integrates an effector target with an NLR complex at the DNA to switch a potent bacterial virulence activity into defense gene activation.

PMID:
26000483
DOI:
10.1016/j.cell.2015.04.025
[Indexed for MEDLINE]
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