Link to home

N-Terminal Motifs in Some Plant Disease Resistance Proteins Function in Membrane Attachment and Contribute to Disease Resistance

March 2012 , Volume 25 , Number  3
Pages  379 - 392

Daigo Takemoto,1 Maryam Rafiqi,1 Ursula Hurley,1 Greg J. Lawrence,2 Maud Bernoux,2 Adrienne R. Hardham,1 Jeffrey G. Ellis,2 Peter N. Dodds,2 and David A. Jones1

1Plant Science Division, Research School of Biology, The Australian National University, Canberra ACT 0200, Australia; 2CSIRO Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia


Go to article:
Accepted 26 October 2011.

To investigate the role of N-terminal domains of plant disease resistance proteins in membrane targeting, the N termini of a number of Arabidopsis and flax disease resistance proteins were fused to green fluorescent protein (GFP) and the fusion proteins localized in planta using confocal microscopy. The N termini of the Arabidopsis RPP1-WsB and RPS5 resistance proteins and the PBS1 protein, which is required for RPS5 resistance, targeted GFP to the plasma membrane, and mutation of predicted myristoylation and potential palmitoylation sites resulted in a shift to nucleocytosolic localization. The N-terminal domain of the membrane-attached Arabidopsis RPS2 resistance protein was targeted incompletely to the plasma membrane. In contrast, the N-terminal domains of the Arabidopsis RPP1-WsA and flax L6 and M resistance proteins, which carry predicted signal anchors, were targeted to the endomembrane system, RPP1-WsA to the endoplasmic reticulum and the Golgi apparatus, L6 to the Golgi apparatus, and M to the tonoplast. Full-length L6 was also targeted to the Golgi apparatus. Site-directed mutagenesis of six nonconserved amino acid residues in the signal anchor domains of L6 and M was used to change the localization of the L6 N-terminal fusion protein to that of M and vice versa, showing that these residues control the targeting specificity of the signal anchor. Replacement of the signal anchor domain of L6 by that of M did not affect L6 protein accumulation or resistance against flax rust expressing AvrL567 but removal of the signal anchor domain reduced L6 protein accumulation and L6 resistance, suggesting that membrane attachment is required to stabilize the L6 protein.



© 2012 The American Phytopathological Society