A plant immune receptor detects pathogen effectors that target WRKY transcription factors

Panagiotis F Sarris; Zane Duxbury; Sung Un Huh; Yan Ma; Cécile Segonzac; Jan Sklenar; Paul Derbyshire; Volkan Cevik; Ghanasyam Rallapalli; Simon B Saucet; Lennart Wirthmueller; Frank L H Menke; Kee Hoon Sohn; Jonathan D G Jones

doi:10.1016/j.cell.2015.04.024

A plant immune receptor detects pathogen effectors that target WRKY transcription factors

Panagiotis F Sarris, Zane Duxbury, Sung Un Huh, Yan Ma, Cécile Segonzac, Jan Sklenar, Paul Derbyshire, Volkan Cevik, Ghanasyam Rallapalli, Simon B Saucet, Lennart Wirthmueller, Frank L H Menke, Kee Hoon Sohn, Jonathan D G Jones

Research output: Contribution to journal › Article › peer-review

388 Citations (SciVal)

Abstract

Defense against pathogens in multicellular eukaryotes depends on intracellular immune receptors, yet surveillance by these receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a "decoy" domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.

Original language	English
Pages (from-to)	1089-1100
Number of pages	12
Journal	Cell
Volume	161
Issue number	5
Early online date	21 May 2015
DOIs	https://doi.org/10.1016/j.cell.2015.04.024
Publication status	Published - 21 May 2015

Keywords

Amino Acid Sequence
Arabidopsis
Arabidopsis Proteins
Bacterial Proteins
Immunity, Innate
Molecular Sequence Data
Plant Proteins
Protein Structure, Tertiary
Pseudomonas fluorescens
Pseudomonas syringae
Tobacco
Journal Article
Research Support, Non-U.S. Gov't

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10.1016/j.cell.2015.04.024Licence: Other

Volkan Cevik
- V.Cevikbath.acuk
- Department of Life Sciences - Senior Lecturer
- Milner Centre for Evolution
Person: Research & Teaching

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title = "A plant immune receptor detects pathogen effectors that target WRKY transcription factors",

abstract = "Defense against pathogens in multicellular eukaryotes depends on intracellular immune receptors, yet surveillance by these receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a {"}decoy{"} domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.",

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author = "Sarris, {Panagiotis F} and Zane Duxbury and Huh, {Sung Un} and Yan Ma and C{\'e}cile Segonzac and Jan Sklenar and Paul Derbyshire and Volkan Cevik and Ghanasyam Rallapalli and Saucet, {Simon B} and Lennart Wirthmueller and Menke, {Frank L H} and Sohn, {Kee Hoon} and Jones, {Jonathan D G}",

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AU - Sarris, Panagiotis F

AU - Duxbury, Zane

AU - Huh, Sung Un

AU - Ma, Yan

AU - Segonzac, Cécile

AU - Sklenar, Jan

AU - Derbyshire, Paul

AU - Cevik, Volkan

AU - Rallapalli, Ghanasyam

AU - Saucet, Simon B

AU - Wirthmueller, Lennart

AU - Menke, Frank L H

AU - Sohn, Kee Hoon

AU - Jones, Jonathan D G

PY - 2015/5/21

Y1 - 2015/5/21

N2 - Defense against pathogens in multicellular eukaryotes depends on intracellular immune receptors, yet surveillance by these receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a "decoy" domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.

AB - Defense against pathogens in multicellular eukaryotes depends on intracellular immune receptors, yet surveillance by these receptors is poorly understood. Several plant nucleotide-binding, leucine-rich repeat (NB-LRR) immune receptors carry fusions with other protein domains. The Arabidopsis RRS1-R NB-LRR protein carries a C-terminal WRKY DNA binding domain and forms a receptor complex with RPS4, another NB-LRR protein. This complex detects the bacterial effectors AvrRps4 or PopP2 and then activates defense. Both bacterial proteins interact with the RRS1 WRKY domain, and PopP2 acetylates lysines to block DNA binding. PopP2 and AvrRps4 interact with other WRKY domain-containing proteins, suggesting these effectors interfere with WRKY transcription factor-dependent defense, and RPS4/RRS1 has integrated a "decoy" domain that enables detection of effectors that target WRKY proteins. We propose that NB-LRR receptor pairs, one member of which carries an additional protein domain, enable perception of pathogen effectors whose function is to target that domain.

KW - Amino Acid Sequence

KW - Arabidopsis

KW - Arabidopsis Proteins

KW - Bacterial Proteins

KW - Immunity, Innate

KW - Molecular Sequence Data

KW - Plant Proteins

KW - Protein Structure, Tertiary

KW - Pseudomonas fluorescens

KW - Pseudomonas syringae

KW - Tobacco

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.cell.2015.04.024

DO - 10.1016/j.cell.2015.04.024

M3 - Article

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SN - 0092-8674

VL - 161

SP - 1089

EP - 1100

JO - Cell

JF - Cell

IS - 5

ER -

A plant immune receptor detects pathogen effectors that target WRKY transcription factors

Abstract

Keywords

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Volkan Cevik

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