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- Publisher
- Wiley
- Copyright
- Copyright © 1999 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 0960-7412
- eISSN
- 1365-313X
- DOI
- 10.1046/j.1365-313X.1999.00451.x
- Publisher site
- See Article on Publisher Site
Abstract
Peptides corresponding to the most conserved domain of eubacterial flagellin act as potent elicitors in cells of different plant species. In intact Arabidposis thaliana seedlings these peptides (flg22 and flg15) caused callose deposition, induction of genes coding for pathogenesis‐related proteins and a strong inhibition of growth. Half‐maximal growth inhibition occurred at peptide concentrations of approximately 100 nM. In contrast, peptides representing the corresponding flagellin domains of the plant‐associated bacteria A. tumefaciens and R. meliloti were inactive even at concentrations of 10 μM. With the exception of Ws‐0, all ecotypes of A. thaliana tested were sensitive to flg22. Crosses of Ws‐0 with the sensitive ecotypes Col‐0 and La‐er, respectively, resulted in sensitive F1 seedlings. In the F2 generation of both crosses, sensitivity segregated as a single trait with markers of chromosome 5 and a ratio of 3:1. Dominance of the locus sensing flagellin, termed FLS‐1, suggests that it encodes an element which is important for the perception of the flagellin signal.
Journal
The Plant Journal – Wiley
Published: May 1, 1999