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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.

Original publication




Journal article


Mol Plant Microbe Interact

Publication Date





412 - 415


Amino Acid Motifs, Amino Acid Substitution, Cell Membrane, Cladosporium, Dipeptides, Endoplasmic Reticulum, Fungal Proteins, Lycopersicon esculentum, Membrane Glycoproteins, Mutagenesis, Plant Proteins, Protein Binding, Sequence Analysis, Protein, Structure-Activity Relationship