The C-terminal dilysine motif for targeting to the endoplasmic reticulum is not required for Cf-9 function.
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.
Laboratory of Phytopathology, Wageningen University, The Netherlands.
R A
RA
van der Hoorn
A
A
Ven der Ploeg
P J
PJ
de Wit
M H
MH
Joosten
D020816:Amino Acid Motifs; D019943:Amino Acid Substitution; D002462:Cell Membrane / Q000378:metabolism; D002963:Cladosporium / Q000378:metabolism; D004151:Dipeptides / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D018551:Solanum lycopersicum / Q000235:genetics / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D016296:Mutagenesis; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D020539:Sequence Analysis, Protein; D013329:Structure-Activity Relationship
D004151:Dipeptides; D005656:Fungal Proteins; D008562:Membrane Glycoproteins; D010940:Plant Proteins; C073605:AVR9 protein, Cladosporium fulvum; C024575:lysyllysine