The integrated LIM-peptidase domain of the CSA1-CHS3/DAR4 paired immune receptor detects changes in DA1 peptidase inhibitors in Arabidopsis

Gu, Benguo, Parkes, Toby, Rabanal, Fernando, Smith, Caroline, Lu, Fu-Hao, McKenzie, Neil, Dong, Hui, Weigel, Detlef, Jones, Jonathan D. G., Cevik, Volkan and Bevan, Michael W. (2023) The integrated LIM-peptidase domain of the CSA1-CHS3/DAR4 paired immune receptor detects changes in DA1 peptidase inhibitors in Arabidopsis. Cell Host & Microbe, 31 (6). 949-961.e5. ISSN 1931-3128

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Abstract

White blister rust, caused by the oomycete Albugo candida, is a widespread disease of Brassica crops. The Brassica relative Arabidopsis thaliana uses the paired immune receptor complex CSA1-CHS3/DAR4 to resist Albugo infection. The CHS3/DAR4 sensor NLR, which functions together with its partner, the helper NLR CSA1, carries an integrated domain (ID) with homology to DA1 peptidases. Using domain swaps with several DA1 homologs, we show that the LIM-peptidase domain of the family member CHS3/DAR4 functions as an integrated decoy for the family member DAR3, which interacts with and inhibits the peptidase activities of the three closely related peptidases DA1, DAR1, and DAR2. Albugo infection rapidly lowers DAR3 levels and activates DA1 peptidase activity, thereby promoting endoreduplication of host tissues to support pathogen growth. We propose that the paired immune receptor CSA1-CHS3/DAR4 detects the actions of a putative Albugo effector that reduces DAR3 levels, resulting in defense activation.

Item Type:	Article
Additional Information:	Data and code availability: • Sequences of CSA1, CHS3/DAR4, DA1 and DAR3 are publicly available from Genbank. Accession numbers are listed in the key resources table. All data generated in this study are in Tables S1–S16. • No original code was used in this study. •Any additional information required to re-analyze the data reported in this paper is available from the lead contact upon request. Funding information: This work was funded by the Biological and Biotechnological Sciences Research Council (BBSRC) Newton Fund to B.G. and M.W.B., BBSRC grant BB/K017225 to M.W.B., and Institute Strategic Grant GEN (BB/P013511/1) to M.W.B. Work in the J.D.G.J. lab was supported by a Gatsby Charitable Foundation grant to TSL Norwich, by BBSRC BB/M003809/1 (supported V.C.) and ERC grant 233376 “Albugon” (supported VK). Work in the V.C. lab was supported by the University of Bath University Research Studentship Account (URSA), University of Bath start-up fund, and Royal Society International Collaboration Awards (ICA∖R1∖201511). We thank the 1001 Genomes Plus (1001G+) project, funded by ERA-CAPS through BBSRC, DFG, and FWF to Paul Kersey, Detlef Weigel, and Magnus Nordborg, for access to newly assembled Arabidopsis genomes.
Faculty \ School:	Faculty of Science > School of Biological Sciences Faculty of Science > The Sainsbury Laboratory
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	LivePure Connector
Date Deposited:	18 May 2023 11:31
Last Modified:	24 Oct 2023 01:39
URI:	https://ueaeprints.uea.ac.uk/id/eprint/92096
DOI:	10.1016/j.chom.2023.04.009

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