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XCP1 cleaves Pathogenesis-related protein 1 into CAPE9 for systemic immunity in Arabidopsis

ABSTRACT: This repository is related to the work” XCP1 cleaves Pathogenesis-related protein 1 into CAPE9 for systemic immunity in Arabidopsis”. In this study, we found that the C-terminal proteolytic processing of a caspase-like substrate motif “CNYD” within Pathogenesis-related protein 1 (PR1) generates an immunomodulatory cytokine (CAPE9) in Arabidopsis. Salicylic acid enhances CNYD-targeted protease activity and the proteolytic release of CAPE9 from PR1 in Arabidopsis. This process involves a protease exhibiting caspase-like enzyme activity, identified as Xylem cysteine peptidase 1 (XCP1). XCP1 exhibits a calcium-modulated pH-activity profile and a comparable activity to human caspases. XCP1 is required to induce systemic immunity triggered by pathogen-associated molecular patterns. This work reveals XCP1 as a key protease for plant immunity, which produces the cytokine CAPE9 from the canonical salicylic acid signaling marker PR1 to activate systemic immunity. The following files are stored here: one MS datasets (include .raw, preprocessed .mgf, and Mascot MS/MS ion search result .dat file) generated in this work, including: “Total identified endogenous peptides observed in SA-treated Arabidopsis leaves on Q Exactive HF (named as supplementaldata2)”

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Leaf

SUBMITTER: Shengchi Hung

LAB HEAD: Yet Ran Chen

PROVIDER: PXD041898 | Pride | 2023-07-20

REPOSITORIES: Pride

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			Action	DRS
	SupplementalData2_200220_Cindee_QEHF_Arab_Pep_SA_DDA2_F16.mgf	Mgf
	SupplementalData2_200220_Cindee_QEHF_Arab_Pep_SA_DDA2_F16.raw	Raw
	SupplementalData2_Peptidome_IDResult_MASCOT.dat	Other
	checksum.txt	Txt

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XCP1 cleaves Pathogenesis-related protein 1 into CAPE9 for systemic immunity in Arabidopsis

Project description:This repository is related to the work: XCP1 cleaves Pathogenesis-related protein 1 into CAPE9 for systemic immunity in Arabidopsis. In this study, we found that the C-terminal proteolytic processing of a caspase-like substrate motif CNYD within Pathogenesis-related protein 1 (PR1) generates an immunomodulatory cytokine (CAPE9) in Arabidopsis. Salicylic acid enhances CNYD-targeted protease activity and the proteolytic release of CAPE9 from PR1 in Arabidopsis. This process involves a protease exhibiting caspase-like enzyme activity, identified as Xylem cysteine peptidase 1 (XCP1). XCP1 exhibits a calcium-modulated pH-activity profile and a comparable activity to human caspases. XCP1 is required to induce systemic immunity triggered by pathogen-associated molecular patterns. This work reveals XCP1 as a key protease for plant immunity, which produces the cytokine CAPE9 from the canonical salicylic acid signaling marker PR1 to activate systemic immunity The following files are stored here: four MS datasets (.raw files)generated in this work, including: (1) The SA contents in Arabidopsis treated with water or AtCAPE9 on Orbitrap Elite (fig1a); (2) MS/MS spectra of endogenous and synthetic AtCAPE9 on Orbitrap Elite (fig1b); (3) Quantification of endogenous AtCAPE9 in Arabidopsis leaves with or without SA treatment on Orbitrap Elite (fig3a); (4) Quantification of endogenous AtCAPE9 in WT or xcp1 Arabidopsis leaves treated with SA on Orbitrap LTQ XL (figS7c)

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