Analysis of structure and function of RPS4 and RRS1 proteins

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We found that both Arabidopsis RRS1 and RPS4 are required for resistance to Colletotrichum higginsianum, Ralstonia solanacearum and Pseudomonas syringae pv. tomato strain DC3000 expressing avrRps4.These two adjacent R genes confer resistance, in tandem or individually, to three distinct pathogens with very different infection strategies and virulence mechanisms. The comparison of amino acid sequences of the RPS4 alleles from twenty ecotypes revealed the protein sequences were highly similar. On the contrary, we found several variations in the LRR domain and C-terminal region of RRS1 by comparing twenty ecotypes. Natural variation in receptor-type R proteins often occurs in their LRR domain, typically at the solvent exposedβ-strand/β-turn structure. The strong selection pressure at the LRR domain suggests that this is the domain directly binds to the pathogen determinants that are evolving fast. We introduced some amino acid changes into RPS4 and RRS1, and we revealed the structure and function of RPS4 and RRS1 proteins.