Plant receptor-like protein activation by a microbial glycoside hydrolase
Yue Sun,
Yan Wang (),
Xiaoxiao Zhang,
Zhaodan Chen,
Yeqiang Xia,
Lei Wang,
Yujing Sun,
Mingmei Zhang,
Yu Xiao,
Zhifu Han (),
Yuanchao Wang () and
Jijie Chai ()
Additional contact information
Yue Sun: Tsinghua University
Yan Wang: Nanjing Agricultural University
Xiaoxiao Zhang: Tsinghua University
Zhaodan Chen: Nanjing Agricultural University
Yeqiang Xia: Nanjing Agricultural University
Lei Wang: Nanjing Agricultural University
Yujing Sun: Nanjing Agricultural University
Mingmei Zhang: Nanjing Agricultural University
Yu Xiao: Tsinghua University
Zhifu Han: Tsinghua University
Yuanchao Wang: Nanjing Agricultural University
Jijie Chai: Tsinghua University
Nature, 2022, vol. 610, issue 7931, 335-342
Abstract:
Abstract Plants rely on cell-surface-localized pattern recognition receptors to detect pathogen- or host-derived danger signals and trigger an immune response1–6. 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 immunity1–3. 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.
Date: 2022
References: Add references at CitEc
Citations: View citations in EconPapers (2)
Downloads: (external link)
https://www.nature.com/articles/s41586-022-05214-x Abstract (text/html)
Access to the full text of the articles in this series is restricted.
Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.
Export reference: BibTeX
RIS (EndNote, ProCite, RefMan)
HTML/Text
Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:610:y:2022:i:7931:d:10.1038_s41586-022-05214-x
Ordering information: This journal article can be ordered from
https://www.nature.com/
DOI: 10.1038/s41586-022-05214-x
Access Statistics for this article
Nature is currently edited by Magdalena Skipper
More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().