A receptor pair with an integrated decoy converts pathogen disabling of transcription factors to immunity

Cell. 2015 May 21;161(5):1074-1088. doi: 10.1016/j.cell.2015.04.025.


Microbial pathogens infect host cells by delivering virulence factors (effectors) that interfere with defenses. In plants, intracellular nucleotide-binding/leucine-rich repeat receptors (NLRs) detect specific effector interference and trigger immunity by an unknown mechanism. The Arabidopsis-interacting NLR pair, RRS1-R with RPS4, confers resistance to different pathogens, including Ralstonia solanacearum bacteria expressing the acetyltransferase effector PopP2. We show that PopP2 directly acetylates a key lysine within an additional C-terminal WRKY transcription factor domain of RRS1-R that binds DNA. This disrupts RRS1-R DNA association and activates RPS4-dependent immunity. PopP2 uses the same lysine acetylation strategy to target multiple defense-promoting WRKY transcription factors, causing loss of WRKY-DNA binding and transactivating functions needed for defense gene expression and disease resistance. Thus, RRS1-R integrates an effector target with an NLR complex at the DNA to switch a potent bacterial virulence activity into defense gene activation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetyltransferases / metabolism
  • Arabidopsis / immunology*
  • Arabidopsis / microbiology
  • Arabidopsis Proteins / metabolism
  • DNA / metabolism
  • Models, Molecular
  • Plant Proteins / metabolism
  • Ralstonia solanacearum / enzymology
  • Ralstonia solanacearum / metabolism
  • Ralstonia solanacearum / pathogenicity
  • Transcription Factors / metabolism


  • Arabidopsis Proteins
  • Plant Proteins
  • RRS1 protein, Arabidopsis
  • Transcription Factors
  • rps4 protein, plant
  • DNA
  • Acetyltransferases