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United States Department of Agriculture

Agricultural Research Service

Research Project: POTATO GERMPLASM ENHANCEMENT THROUGH TRAIT DISCOVERY, GENETIC EVALUATION AND INCORPORATION Title: Enhanced Disease Susceptibility 1 and Salicylic Acid Act Redundantly to Regulate Resistance Gene-Mediated Signaling

Authors
item Venugopal, Srivathsa - UNIVERSITY OF KENTUCKY
item Jeong, Rae-Dong - UNIVERSITY OF KENTUCKY
item Chandra-Shekara, A - UNIVERSITY OF KENTUCKY
item Zhu, Shifeng - UNIVERSITY OF KENTUCKY
item Mandal, Mihir - UNIVERSITY OF KENTUCKY
item Hersh, Matthew - UNIVERSITY OF KENTUCKY
item Stromberg, Arnold - UNIVERSITY OF KENTUCKY
item Navarre, Duroy
item Kachroo, Aardra - UNIVERSITY OF KENTUCKY
item Kachroo, Pradeep - UNIVERSITY OF KENTUCKY

Submitted to: PLoS Genetics
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: February 2, 2009
Publication Date: June 1, 2009
Citation: Venugopal, S.C., Jeong, R., Chandra-Shekara, A.C., Zhu, S., Mandal, M., Hersh, M., Stromberg, A.J., Navarre, D.A., Kachroo, A., Kachroo, P. 2009. ENHANCED DISEASE SUSCEPTIBILITY 1 and SALICYLIC ACID act redundantly to regulate resistance gene-mediated signaling. PLoS Genetics. 5(7): e1000545 DOI:10.1371/journal.pgen.1000545.

Interpretive Summary: This research shows that salicylic acid and EDS1 have redundant function in resistance gene induction and resistance to bacterial, viral and oomycete plant pathogens. This helps us better understand R-gene mediated defense signaling, a major mechanism by which plants resist disease.

Technical Abstract: Resistance (R) protein–associated pathways are well known to participate in defense against a variety of microbial pathogens. Salicylic acid (SA) and its associated proteinaceous signaling components, including enhanced disease susceptibility 1 (EDS1), non–race-specific disease resistance 1 (NDR1), phytoalexin deficient 4 (PAD4), senescence associated gene 101 (SAG101), and EDS5, have been identified as components of resistance derived from many R proteins. Here, we show that EDS1 and SA fulfill redundant functions in defense signaling mediated by R proteins, which were thought to function independent of EDS1 and/or SA. Simultaneous mutations in EDS1 and the SA–synthesizing enzyme SID2 compromised hypersensitive response and/or resistance mediated by R proteins that contain coiled coil domains at their N-terminal ends. Furthermore, the expression of R genes and the associated defense signaling induced in response to a reduction in the level of oleic acid were also suppressed by compromising SA biosynthesis in the eds1 mutant background. The functional redundancy with SA was specific to EDS1. Results presented here redefine our understanding of the roles of EDS1 and SA in plant defense.

Last Modified: 11/20/2014