4.5 Article

The C-terminal dilysine motif for targeting to the endoplasmic reticulum is not required for Cf-9 function

Journal

MOLECULAR PLANT-MICROBE INTERACTIONS
Volume 14, Issue 3, Pages 412-415

Publisher

AMER PHYTOPATHOLOGICAL SOC
DOI: 10.1094/MPMI.2001.14.3.412

Keywords

avirulence gene; CLAVATA; ER retention; ER retrieval; high-affinity binding site

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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.

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