Document Detail

Arabidopsis lysin-motif proteins LYM1 LYM3 CERK1 mediate bacterial peptidoglycan sensing and immunity to bacterial infection.
MedLine Citation:
PMID:  22106285     Owner:  NLM     Status:  MEDLINE    
Recognition of microbial patterns by host pattern recognition receptors is a key step in immune activation in multicellular eukaryotes. Peptidoglycans (PGNs) are major components of bacterial cell walls that possess immunity-stimulating activities in metazoans and plants. Here we show that PGN sensing and immunity to bacterial infection in Arabidopsis thaliana requires three lysin-motif (LysM) domain proteins. LYM1 and LYM3 are plasma membrane proteins that physically interact with PGNs and mediate Arabidopsis sensitivity to structurally different PGNs from gram-negative and gram-positive bacteria. lym1 and lym3 mutants lack PGN-induced changes in transcriptome activity patterns, but respond to fungus-derived chitin, a pattern structurally related to PGNs, in a wild-type manner. Notably, lym1, lym3, and lym3 lym1 mutant genotypes exhibit supersusceptibility to infection with virulent Pseudomonas syringae pathovar tomato DC3000. Defects in basal immunity in lym3 lym1 double mutants resemble those observed in lym1 and lym3 single mutants, suggesting that both proteins are part of the same recognition system. We further show that deletion of CERK1, a LysM receptor kinase that had previously been implicated in chitin perception and immunity to fungal infection in Arabidopsis, phenocopies defects observed in lym1 and lym3 mutants, such as peptidoglycan insensitivity and enhanced susceptibility to bacterial infection. Altogether, our findings suggest that plants share with metazoans the ability to recognize bacterial PGNs. However, as Arabidopsis LysM domain proteins LYM1, LYM3, and CERK1 form a PGN recognition system that is unrelated to metazoan PGN receptors, we propose that lineage-specific PGN perception systems have arisen through convergent evolution.
Roland Willmann; Heini M Lajunen; Gitte Erbs; Mari-Anne Newman; Dagmar Kolb; Kenichi Tsuda; Fumiaki Katagiri; Judith Fliegmann; Jean-Jacques Bono; Julie V Cullimore; Anna K Jehle; Friedrich Götz; Andreas Kulik; Antonio Molinaro; Volker Lipka; Andrea A Gust; Thorsten Nürnberger
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2011-11-21
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  108     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2011-12-07     Completed Date:  2012-04-13     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  19824-9     Citation Subset:  IM    
Department of Plant Biochemistry, Center for Plant Molecular Biology, University of Tübingen, 72076 Tübingen, Germany.
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MeSH Terms
Arabidopsis / genetics,  metabolism,  microbiology
Arabidopsis Proteins / classification,  genetics,  metabolism*
Bacteria / growth & development,  immunology,  metabolism*
Disease Resistance / genetics,  immunology
Gene Expression Regulation, Plant
Green Fluorescent Proteins / genetics,  metabolism
Host-Pathogen Interactions / immunology
Microscopy, Confocal
Oligonucleotide Array Sequence Analysis
Peptidoglycan / immunology,  metabolism*
Plant Diseases / genetics,  immunology,  microbiology
Plants, Genetically Modified
Protein-Serine-Threonine Kinases / genetics,  metabolism*
Pseudomonas syringae / immunology,  metabolism,  physiology
Reverse Transcriptase Polymerase Chain Reaction
Staphylococcus aureus / immunology,  metabolism,  physiology
Reg. No./Substance:
0/Arabidopsis Proteins; 0/LYM1 protein, Arabidopsis; 0/LYM3 protein, Arabidopsis; 0/Peptidoglycan; 147336-22-9/Green Fluorescent Proteins; EC protein, Arabidopsis; EC Kinases

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