Universität zu Köln

Sun, Yue, Wang, Yan ORCID: 0000-0001-7465-5518, Zhang, Xiaoxiao ORCID: 0000-0003-3762-2287, Chen, Zhaodan, Xia, Yeqiang, Wang, Lei, Sun, Yujing, Zhang, Mingmei, Xiao, Yu, Han, Zhifu, Wang, Yuanchao and Chai, Jijie (2022). Plant receptor-like protein activation by a microbial glycoside hydrolase. Nature, 610 (7931). S. 335 - 362. BERLIN: NATURE PORTFOLIO. ISSN 1476-4687

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Abstract

Plants rely on cell-surface-localized pattern recognition receptors to detect pathogen- or host-derived danger signals and trigger an immune response(1-6). Receptor-like proteins (RLPs) with a leucine-rich repeat (LRR) ectodomain constitute a subgroup of pattern recognition receptors and play a critical role in plant immunity(1-3). Mechanisms underlying ligand recognition and activation of LRR-RLPs remain elusive. Here we report a crystal structure of the LRR-RLP RXEG1 from Nicotiana benthamiana that recognizes XEG1 xyloglucanase from the pathogen Phytophthora sojae. The structure reveals that specific XEG1 recognition is predominantly mediated by an amino-terminal and a carboxy-terminal loop-out region (RXEG1(ID)) of RXEG1. The two loops bind to the active-site groove of XEG1, inhibiting its enzymatic activity and suppressing Phytophthora infection of N. benthamiana. Binding of XEG1 promotes association of RXEG1(LRR) with the LRR-type co-receptor BAK1 through RXEG1(ID) and the last four conserved LRRs to trigger RXEG1-mediated immune responses. Comparison of the structures of apo-RXEG1(LRR), XEG1-RXEG1(LRR) and XEG1-BAK1-RXEG1(LRR) shows that binding of XEG1 induces conformational changes in the N-terminal region of RXEG1(ID) and enhances structural flexibility of the BAK1-associating regions of RXEG1(LRR). These changes allow fold switching of RXEG1(ID) for recruitment of BAK1(LRR). Our data reveal a conserved mechanism of ligand-induced heterodimerization of an LRR-RLP with BAK1 and suggest a dual function for the LRR-RLP in plant immunity.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Sun, Yue UNSPECIFIED UNSPECIFIED UNSPECIFIED Wang, Yan UNSPECIFIED orcid.org/0000-0001-7465-5518 UNSPECIFIED Zhang, Xiaoxiao UNSPECIFIED orcid.org/0000-0003-3762-2287 UNSPECIFIED Chen, Zhaodan UNSPECIFIED UNSPECIFIED UNSPECIFIED Xia, Yeqiang UNSPECIFIED UNSPECIFIED UNSPECIFIED Wang, Lei UNSPECIFIED UNSPECIFIED UNSPECIFIED Sun, Yujing UNSPECIFIED UNSPECIFIED UNSPECIFIED Zhang, Mingmei UNSPECIFIED UNSPECIFIED UNSPECIFIED Xiao, Yu UNSPECIFIED UNSPECIFIED UNSPECIFIED Han, Zhifu UNSPECIFIED UNSPECIFIED UNSPECIFIED Wang, Yuanchao UNSPECIFIED UNSPECIFIED UNSPECIFIED Chai, Jijie UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-680197
DOI:	10.1038/s41586-022-05214-x
Journal or Publication Title:	Nature
Volume:	610
Number:	7931
Page Range:	S. 335 - 362
Date:	2022
Publisher:	NATURE PORTFOLIO
Place of Publication:	BERLIN
ISSN:	1476-4687
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language ETHYLENE-INDUCING XYLANASE; STRUCTURAL BASIS; INNATE IMMUNITY; KINASE; PERCEPTION; RECOGNITION; INSIGHT; COMPLEX; BAK1 Multiple languages Multidisciplinary Sciences Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/68019