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December 4, 2020Science512 citations

Direct pathogen-induced assembly of an NLR immune receptor complex to form a holoenzyme

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MSMa ShouCaiDLDmitry LapinJLJie Liu

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Abstract

Tetrameric immune receptors Nucleotide-binding/leucine-rich repeat (NLR) immune receptors detect pathogen effectors and trigger a plant's immune response. Two groups have now defined the structures of two NLRs that carry Toll-like interleukin-1 receptor (TIR) domains (TIR-NLRs) (see the Perspective by Tian and Li). Ma et al. studied the Arabidopsis thaliana TIR-NLR RPP1 (recognition of Peronospora parasitica 1) and its response to effectors from an oomycete pathogen. Martin et al. studied the Nicotiana benthamiana TIR-NLR ROQ1 (recognition of XopQ 1) and its response to the Xanthomonas effector. Both groups found that these TIR-NLRs formed tetramers that, when activated by binding to the pathogen effector, exposed the active site of a nicotinamide adenine dinucleoside (NAD) hydrolase. Thus, recognition of the pathogen effector initiates NAD hydrolysis and begins the immune response. Science , this issue p. eabe3069 , p. eabd9993 ; see also p. 1163

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ShouCai et al. (2020) studied this question.

synapsesocial.com/papers/6a6197e198d8cb904426dea0https://doi.org/10.1126/science.abe3069
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