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Identification ofendogenous small peptides involved in rice immunity through transcriptomics- and proteomics-based screening.
Tuesday, 2019/07/30 | 08:27:55

Wang P, Yao S, Kosami KI, Guo T, Li J, Zhang Y, Fukao Y, Kaneko-Kawano T, Zhang H, She YM, Wang P, Xing W, Hanada K, Liu R, Kawano Y.

Plant Biotechnol J. 2019 Jul 13. doi: 10.1111/pbi.13208.

Abstract

Small signaling peptides, generated from larger protein precursors, are important components to orchestrate various plant processes such as development and immune responses. However, small signaling peptides involved in plant immunity remain largely unknown. Here, we developed a pipeline using transcriptomicsand proteomics-based screening to identify putative precursors of small signaling peptides:small secreted proteins (SSPs) in rice, induced by rice blast fungus Magnaportheoryzaeand its elicitor, chitin. We identified 236 SSPs including members of two known small signalingpeptide familiesnamely rapid alkalinization factors and phytosulfokines, as well as many other protein families that are known to be involved in immunity, such as proteinase inhibitors and pathogenesis-related protein families. We also isolated 52 unannotated SSPs, and among them, we found one gene which we namedimmune response peptide(IRP)that appeared to encode the precursor of a small signalingpeptide regulating rice immunity. In rice suspension cells, the expression of IRPwas induced by bacterial peptidoglycan andfungal chitin.Overexpression of IRP enhanced the expression of adefence gene, PAL1and induced the activation of the MAPKs inrice cells. Moreover, the IRP protein level increased insuspension cell medium after chitin treatment. Collectively, we established a simple and efficient pipelineto discover SSPcandidates that may play important roles in rice immunity, and identified 52 unannotated SSPs that may be useful for further elucidation of rice immunity. Our method may be applied to identify SSPs that are involved not only in immunity but also in other plant functions. This article is protected by copyright. All rights reserved.

 

See https://www.ncbi.nlm.nih.gov/pubmed/31301098

Figure 6: IRP is involved in rice immunity

(a) Protein alignment of IRPand its homologues. Predicted N-terminal signal sequences are in a blue box. (b) IRPexpression was induced in suspension cells treated withchitin orPGN. Theexpressionlevelof IRPwas quantified by qRT-PCR with six biological replicates.Error bars indicateS.E. Statistically significant differences betweenthemock and chitin treated cells are depicted with asterisks (*, P< 0.05; **, P< 0.01 and ***, P< 0.001) according to the two-tailed t-test.(c) Effect of overexpression of IRPon the defence gene PAL1. Rice suspension cells overexpressing IRPwere treated with chitin for 1 h. #1 and #2 are two independent lines of transgenic rice suspension cells expressing IRP. Theexpressionlevels of IRPand PAL1were quantified by qRT-PCR with fourindependent replicates.Error bars indicateS.E. Statisticallysignificant differences between wild-type (WT) and overexpression lines are depicted with asterisks (*, P< 0.05; **, P< 0.01 and ***, P< 0.001) according to the two-tailed t-test.(d) Overexpression of IRPinduces MAPK activation.MAPK activation was detected in WT and IRPoverexpression lines #1 and #2 suspension cells using anti-phospho-p44/42 MAPK antibody. CBB, Coomassie brilliant blue.(e) The protein abundanceof IRPin the mediumincreased following chitinexposure. The 20-aa peptide GEGWLEDGIGMVVDMLGELKof IRPwas used as a spectral to matchthe MS/MS spectrum of the peptide acquired using theparallel reaction monitoring (PRM) method. The rice suspension cellswere treated with chitin for 2 h intwo independent experiments. The total intensity of the peptide in the medium was determined in the mock and chitin treatedsample, respectively. Error bars indicateS.E. Statistically significant differences between themockand chitin treatmentsare depicted with asterisks (***, P< 0.001) according to the two-tailed t-test.

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