Open AccessThe C-terminal Dilysine Motif for Targeting to the Endoplasmic Reticulum Is Not Required for Cf-9 Function
Author(s) -
R.A.L. van der Hoorn,
A. van der Ploeg,
P.J.G.M. de Wit,
M.H.A.J. Joosten
Publication year - 2001
Publication title -
molecular plant-microbe interactions
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.565
H-Index - 153
eISSN - 1943-7706
pISSN - 0894-0282
DOI - 10.1094/mpmi.2001.14.3.412
Subject(s) - endoplasmic reticulum , microbiology and biotechnology , subcellular localization , mutant , extracellular , protein sorting signals , stim1 , transport protein , biology , gene , chemistry , biochemistry , peptide sequence , signal peptide
The tomato resistance gene Cf-9 encodes a membrane-anchored, receptor-like protein that mediates specific recognition of the extracellular elicitor protein AVR9 of Cladosporium fulvum. The C-terminal dilysine motif (KKRY) of Cf-9 suggests that the protein resides in the endoplasmic reticulum. Previously, two conflicting reports on the subcellular location of Cf-9 were published. Here we show that the AARY mutant version of Cf-9 is still functional in mediating AVR9 recognition, suggesting that functional Cf-9 resides in the plasma membrane. The data presented here and in reports by others can be explained by masking the dilysine signal of Cf-9 with other proteins.