气候变化领域集成服务门户(CCPortal): Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor

CCPortal

DOI	10.1073/pnas.2113996118
	Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor
	Mukhi N.; Brown H.; Gorenkin D.; Ding P.; Bentham A.R.; Stevenson C.E.M.; Jones J.D.G.; Banfield M.J.
发表日期	2021
ISSN	0027-8424
卷号	118 期号:50
英文摘要	Plants use intracellular nucleotide-binding domain (NBD) and leucine-rich repeat (LRR)–containing immune receptors (NLRs) to detect pathogen-derived effector proteins. The Arabidopsis NLR pair RRS1-R/RPS4 confers disease resistance to different bacterial pathogens by perceiving the structurally distinct effectors AvrRps4 from Pseudomonas syringae pv. pisi and PopP2 from Ralstonia solanacearum via an integrated WRKY domain in RRS1-R. How the WRKY domain of RRS1 (RRS1WRKY) perceives distinct classes of effector to initiate an immune response is unknown. Here, we report the crystal structure of the in planta processed C-terminal domain of AvrRps4 (AvrRps4C) in complex with RRS1WRKY. Perception of AvrRps4C by RRS1WRKY is mediated by the β2-β3 segment of RRS1WRKY that binds an electronegative patch on the surface of AvrRps4C. Structure-based mutations that disrupt AvrRps4C–RRS1WRKY interactions in vitro compromise RRS1/RPS4-dependent immune responses. We also show that AvrRps4C can associate with the WRKY domain of the related but distinct RRS1B/RPS4B NLR pair, and the DNA-binding domain of AtWRKY41, with similar binding affinities and how effector binding interferes with WRKY–Wbox DNA interactions. This work demonstrates how integrated domains in plant NLRs can directly bind structurally distinct effectors to initiate immunity. © 2021 National Academy of Sciences. All rights reserved.
英文关键词	Disease resistance; Effector proteins; Plant biology; Protein structure; Virulence
语种	英语
scopus关键词	nucleotide binding oligomerization domain like receptor; RPS4 protein; RRS1 protein; unclassified drug; virulence factor; Arabidopsis protein; bacterial protein; plant DNA; plant protein; rps4 protein, plant; RRS1 protein, Arabidopsis; Arabidopsis; Article; binding affinity; botany; carboxy terminal sequence; complex formation; controlled study; crystal structure; disease resistance; DNA binding motif; immune response; in vitro study; innate immunity; nonhuman; protein binding; protein DNA interaction; protein domain; protein processing; protein structure; virulence; cell death; gene expression regulation; genetics; immunology; metabolism; microbiology; molecular cloning; molecular model; mutation; protein conformation; Pseudomonas syringae; tobacco; Arabidopsis; Arabidopsis Proteins; Bacterial Proteins; Cell Death; Cloning, Molecular; DNA, Plant; Gene Expression Regulation, Plant; Models, Molecular; Mutation; Plant Proteins; Protein Conformation; Pseudomonas syringae; Tobacco
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/250935
作者单位	Department of Biochemistry and Metabolism, John Innes Centre, Norwich, NR4 7UH, United Kingdom; The Sainsbury Laboratory, University of East Anglia, Norwich, NR4 7UH, United Kingdom
推荐引用方式 GB/T 7714	Mukhi N.,Brown H.,Gorenkin D.,et al. Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor[J],2021,118(50).
APA	Mukhi N..,Brown H..,Gorenkin D..,Ding P..,Bentham A.R..,...&Banfield M.J..(2021).Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor.Proceedings of the National Academy of Sciences of the United States of America,118(50).
MLA	Mukhi N.,et al."Perception of structurally distinct effectors by the integrated WRKY domain of a plant immune receptor".Proceedings of the National Academy of Sciences of the United States of America 118.50(2021).