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The C-terminal Dilysine Motif for Targeting to the Endoplasmic Reticulum Is Not Required for Cf-9 Function

March 2001 , Volume 14 , Number  3
Pages  412 - 415

Renier A. L. Van der Hoorn , Anke Van der Ploeg , Pierre J. G. M. de Wit , and Matthieu H. A. J. Joosten

Laboratory of Phytopathology, Wageningen University, Binnenhaven 9, 6709 PD Wageningen, The Netherlands

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Accepted 29 November 2000.

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.

Additional keywords: avirulence gene, CLAVATA, ER retention, ER retrieval, high-affinity binding site.

© 2001 The American Phytopathological Society