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J. Biol. Chem., Vol. 276, Issue 49, 45669-45676, December 7, 2001
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From the Friedrich Miescher-Institute,
CH-4002 Basel, Switzerland
Flagellin, the main building block of the
bacterial flagellum, acts as potent elicitor of defense responses in
different plant species. Genetic analysis in Arabidopsis
thaliana identified two distinct loci, termed FLS1
and FLS2, that are essential for perception of
flagellin-derived elicitors. FLS2 was found to encode a
leucine-rich repeat transmembrane receptor-like kinase with
similarities to Toll-like receptors involved in the innate immune
system of mammals and insects. Here we used a radiolabeled derivative
of flg22, a synthetic peptide representing the elicitor-active
domain of flagellin, to probe the interaction of flagellin with its
receptor in A. thaliana. The high affinity binding site
detected in intact cells and membrane preparations exhibited
specificity for flagellin-derived peptides with biological
activity as agonists or antagonists of the elicitor
responses. Specific binding activity was measurable in all ecotypes of
A. thaliana that show sensitivity to flagellin but was
barely detectable in the flagellin-insensitive ecotype Ws-0 affected in
FLS1. A strongly impaired binding of flagellin was observed
also in several independent flagellin-insensitive mutants isolated from
the flagellin-sensitive ecotype La-er. In particular, no binding was
found in plants carrying a mutation in the LRR domain of
FLS2. These data indicate that the formation of functional
receptor-binding sites depends on genes encoded by both loci,
FLS1 and FLS2. The tight correlation between
the presence of the binding site and elicitor response provides strong evidence that this binding site acts as the physiological receptor of flagellin.
Sensitivity of Different Ecotypes and Mutants of
Arabidopsis thaliana toward the Bacterial Elicitor
Flagellin Correlates with the Presence of Receptor-binding
Sites*
*
The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Friedrich
Miescher-Institute, P.O. Box 2543, CH-4002 Basel, Switzerland.
Tel.: 41-61-6975240; Fax: 41-61-6974527; E-mail:
Felix@fmi.ch.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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