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Plant Cell Advance Online Publication
Published on July 22, 2005; 10.1105/tpc.105.033910

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Received May 3, 2005
Returned for revision June 14, 2005
Accepted June 15, 2005

Arabidopsis SENESCENCE-ASSOCIATED GENE101 Stabilizes and Signals within an ENHANCED DISEASE SUSCEPTIBILITY1 Complex in Plant Innate Immunity

Bart J. Feys 1, Marcel Wiermer 2, Riyaz A. Bhat 2, Lisa. J. Moisan 3, Nieves Medina-Escobar 2, Christina Neu 2, Adriana Cabral 2, and Jane E. Parker 2*

1 Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom; Department of Biological Sciences, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom
2 Department of Plant-Microbe Interactions, Max-Planck-Institute for Plant Breeding Research, 50829 Cologne, Germany
3 Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom

* To whom correspondence should be addressed. E-mail: parker{at}mpiz-koeln.mpg.de.

Plant innate immunity against invasive biotrophic pathogens depends on the intracellular defense regulator ENHANCED DISEASE SUSCEPTIBILITY1 (EDS1). We show here that Arabidopsis thaliana EDS1 interacts in vivo with another protein, SENESCENCE-ASSOCIATED GENE101 (SAG101), discovered through a proteomic approach to identify new EDS1 pathway components. Together with PHYTOALEXIN-DEFICIENT4 (PAD4), a known EDS1 interactor, SAG101 contributes intrinsic and indispensable signaling activity to EDS1-dependent resistance. The combined activities of SAG101 and PAD4 are necessary for programmed cell death triggered by the Toll-Interleukin-1 Receptor type of nucleotide binding/leucine-rich repeat immune receptor in response to avirulent pathogen isolates and in restricting the growth of normally virulent pathogens. We further demonstrate by a combination of cell fractionation, coimmunoprecipitation, and fluorescence resonance energy transfer experiments the existence of an EDS1-SAG101 complex inside the nucleus that is molecularly and spatially distinct from EDS1-PAD4 associations in the nucleus and cytoplasm. By contrast, EDS1 homomeric interactions were detected in the cytoplasm but not inside the nucleus. These data, combined with evidence for coregulation between individual EDS1 complexes, suggest that dynamic interactions of EDS1 and its signaling partners in multiple cell compartments are important for plant defense signal relay.




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