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

被引：22

作者：

Van der Hoorn, RAL ^{[1
]}

Van der Ploeg, A ^{[1
]}

de Wit, PJGM ^{[1
]}

Joosten, MHAJ ^{[1
]}

机构：

[1] Univ Wageningen & Res Ctr, Phytopathol Lab, NL-6709 PD Wageningen, Netherlands

来源：

MOLECULAR PLANT-MICROBE INTERACTIONS | 2001年 / 14卷 / 03期

关键词：

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

D O I：

10.1094/MPMI.2001.14.3.412

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：412 / 415

页数：4

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