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PMID: 20179141 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

PEPR2 is a second receptor for the Pep1 and Pep2 peptides and contributes to defense responses in Arabidopsis.

The Plant cell ·Vol. 22 ·No. 2 ·2010-02-00 ·Pages 508-22

Yamaguchi Y, Huffaker A, Bryan AC, Tax FE, Ryan CA

Abstract

Pep1 is a 23-amino acid peptide that enhances resistance to a root pathogen, Pythium irregulare. Pep1 and its homologs (Pep2 to Pep7) are endogenous amplifiers of innate immunity of Arabidopsis thaliana that induce the transcription of defense-related genes and bind to PEPR1, a plasma membrane leucine-rich repeat (LRR) receptor kinase. Here, we identify a plasma membrane LRR receptor kinase, designated PEPR2, that has 76% amino acid similarity to PEPR1, and we characterize its role in the perception of Pep peptides and defense responses. Both PEPR1 and PEPR2 were transcriptionally induced by wounding, treatment with methyl jasmonate, Pep peptides, and pathogen-associated molecular patterns. The effects of Pep1 application on defense-related gene induction and enhancement of resistance to Pseudomonas syringae pv tomato DC3000 were partially reduced in single mutants of PEPR1 and PEPR2 and abolished completely in double mutants. Photoaffinity labeling and binding assays using transgenic tobacco (Nicotiana tabacum) cells expressing PEPR1 and PEPR2 clearly demonstrated that PEPR1 is a receptor for Pep1-6 and that PEPR2 is a receptor for Pep1 and Pep2. Our analysis demonstrates differential binding affinities of two receptors with a family of peptide ligands and the corresponding physiological effects of the specific receptor-ligand interactions. Therefore, we demonstrate that, through perception of Peps, PEPR1 and PEPR2 contribute to defense responses in Arabidopsis.

MeSH Terms
Amino Acid Sequence Arabidopsis/metabolism Arabidopsis Proteins/chemistry,metabolism Molecular Sequence Data Peptides/metabolism Photoaffinity Labels Sequence Homology, Amino Acid
Chemicals
Arabidopsis Proteins Peptides Photoaffinity Labels
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Yamaguchi Yube
Institute of Biological Chemistry, Washington State University, Pullman, Washington 99164, USA. [email protected]
Huffaker Alisa
Bryan Anthony C
Tax Frans E
Ryan Clarence A
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1532-298X
DOI
10.1105/tpc.109.068874
Email
[email protected]
Published
2010-02-00
Epub
2010-00-23
Pages
508-22
Language
English
Region
England
NLM ID
9208688
PMCID
PMC2845411
Subset
IM
External Links
PubMed source DOI: 10.1105/tpc.109.068874 PMC Full Text View journal details
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