Animal NLRs provide structural insights into plant NLR function
Adam R. Bentham,Adam R. Bentham,H. Burdett,Peter A. Anderson,Simon J. Williams,Simon J. Williams,Simon J. Williams,Bostjan Kobe +7 more
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TLDR
The similarities and differences between plant and animal NLRs are assessed, and the structural information on the animal NLR pair NAIP/NLRC4 is used to derive a plausible model for plant NLR activation.About:
This article is published in Annals of Botany.The article was published on 2016-08-25 and is currently open access. It has received 85 citations till now.read more
Citations
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Journal ArticleDOI
Intracellular innate immune surveillance devices in plants and animals
TL;DR: It is proposed that NLRs evolved for pathogen-sensing in diverse organisms because the flexible protein domain architecture surrounding the NB-ARC and NACHT domains facilitates evolution of “hair trigger” switches, into which a virtually limitless number of microbial detection platforms can be integrated.
Journal ArticleDOI
Reconstitution and structure of a plant NLR resistosome conferring immunity
Jizong Wang,Meijuan Hu,Jia Wang,Jinfeng Qi,Zhifu Han,Guoxun Wang,Yijun Qi,Hong-Wei Wang,Jianmin Zhou,Jijie Chai,Jijie Chai,Jijie Chai +11 more
TL;DR: Structural, biochemical, andfunctional studies show how a plant immune resistosome complex mediates cell death and disease resistance, and verified the biological relevance of the oligomerized ZAR1-RKS1-PBL2UMP complex induced by dATP or ATP with biochemical, cell-based, and functional assays.
Journal ArticleDOI
Ligand-triggered allosteric ADP release primes a plant NLR complex
Jian Wang,Jian Wang,Meijuan Hu,Sau Lan Wu,Ji Qi,Guoxun Wang,Zhifu Han,Ye Qi,Ning Gao,Hong-Wei Wang,Jianmin Zhou,Jijie Chai,Jijie Chai,Jijie Chai +13 more
TL;DR: The cryo-EM structure of the Zar1-RKS1 complex revealed that intramolecular interactions within ZAR1 maintain the NLR protein in an inactive state, and how PBL2UMP affects the ADP-binding activity of theZAR1- R KS1 complex was determined by radiolabeled assays.
Journal ArticleDOI
Differential regulation of TNL-mediated immune signaling by redundant helper CNLs
Zhongshou Wu,Meng Li,Oliver Xiaoou Dong,Shitou Xia,Wanwan Liang,Yongkang Bao,Geoffrey O. Wasteneys,Xin Li +7 more
TL;DR: Through CRISPR/Cas9 gene editing methods, it is discovered that the tandemly repeated NRG1A andNRG1B are functionally redundant and operate downstream of TNLs with differential strengths, suggesting a cytosolic activation mechanism contributing to TNL-specific immunity.
Journal ArticleDOI
NRG1 functions downstream of EDS1 to regulate TIR-NLR-mediated plant immunity in Nicotiana benthamiana
Tiancong Qi,Kyungyong Seong,Daniela P. T. Thomazella,Joonyoung Ryan Kim,Julie Pham,Eunyoung Seo,Myeong-Je Cho,Alex Schultink,Brian J. Staskawicz +8 more
TL;DR: This study demonstrates that NRG1 is a key component that acts downstream of EDS1 to mediate various TNL signaling pathways, including Roq1 and RPP1-mediated HR, resistance to Xanthomonas and Pseudomonas, and XopQ-regulated transcriptional changes in N. benthamiana.
References
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The plant immune system
TL;DR: A detailed understanding of plant immune function will underpin crop improvement for food, fibre and biofuels production and provide extraordinary insights into molecular recognition, cell biology and evolution across biological kingdoms.
Journal ArticleDOI
Toll-like receptor signalling
Shizuo Akira,Kiyoshi Takeda +1 more
TL;DR: Rapid progress that has recently improved the understanding of the molecular mechanisms that mediate TLR signalling is reviewed.
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A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
TL;DR: The cloning and characterization of a human homologue of the Drosophila toll protein (Toll) is reported, which has been shown to induce the innate immune response in adult Dosophila.
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TL;DR: The current knowledge of recognition-dependent disease resistance in plants is reviewed, and a few crucial concepts are included to compare and contrast plant innate immunity with that more commonly associated with animals.
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Apaf-1, a Human Protein Homologous to C. elegans CED-4, Participates in Cytochrome c–Dependent Activation of Caspase-3
TL;DR: The purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3, leading to apoptosis is reported here.
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