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A novel simple extracellular leucine‐rich repeat (eLRR) domain protein from rice (OsLRR1) enters the endosomal pathway and interacts with the hypersensitive‐induced reaction protein 1 (OsHIR1)
Author(s) -
ZHOU LIANG,
CHEUNG MINGYAN,
ZHANG QI,
LEI CAILIN,
ZHANG SHIHONG,
SUN SAMUEL SAIMING,
LAM HONMING
Publication year - 2009
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.2009.02039.x
Subject(s) - leucine rich repeat , biology , subcellular localization , microbiology and biotechnology , protein kinase domain , transmembrane protein , arabidopsis thaliana , protein domain , signal transduction , hypersensitive response , transmembrane domain , extracellular , endosome , fusion protein , arabidopsis , function (biology) , protein kinase a , cytoplasm , kinase , biochemistry , gene , plant disease resistance , receptor , mutant , intracellular , recombinant dna
Receptor‐like protein kinases (RLKs) containing an extracellular leucine‐rich repeat (eLRR) domain, a transmembrane domain and a cytoplasmic kinase domain play important roles in plant disease resistance. Simple eLRR domain proteins structurally resembling the extracellular portion of the RLKs may also participate in signalling transduction and plant defence response. Yet the molecular mechanisms and subcellular localization in regulating plant disease resistance of these simple eLRR domain proteins are still largely unclear. We provided the first experimental evidence to demonstrate the subcellular localization and trafficking of a novel simple eLRR domain protein (OsLRR1) in the endosomal pathway, using both confocal and electron microscopy. Yeast two‐hybrid and in vitro pull‐down assays show that OsLRR1 interacts with the rice hypersensitive‐induced response protein 1 (OsHIR1) which is localized on plasma membrane. The interaction between LRR1 and HIR1 homologs was shown to be highly conserved among different plant species, suggesting a close functional relationship between the two proteins. The function of OsLRR1 in plant defence response was examined by gain‐of‐function tests using transgenic Arabidopsis thaliana . The protective effects of OsLRR1 against bacterial pathogen infection were shown by the alleviating of disease symptoms, lowering of pathogen titres and higher expression of defence marker genes.