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Submitted on February 25, 2008
Accepted on July 2, 2008
Plant Immunity Requires Conformational Changes of NPR1 via S-Nitrosylation and Thioredoxins
Yasuomi Tada 1,Steven H. Spoel 1,Karolina Pajerowska-Mukhtar 1,Zhonglin Mou 2,Junqi Song 1,Xinnian Dong 1*
1 Department of Biology, P.O. Box 90338, Duke University, Durham, NC 27708, USA. 2 Present address: Department of Microbiology and Cell Science, P.O. Box 110700, University of Florida, Gainesville, FL 32611, USA.; Department of Biology, P.O. Box 90338, Duke University, Durham, NC 27708, USA.
* To whom correspondence should be addressed.
Xinnian Dong , E-mail: xdong{at}duke.edu
Changes in redox status have been observed during immune responsesin different organisms, but the associated signaling mechanismsare poorly understood. In plants, these redox changes regulatethe conformation of NPR1, a master regulator of salicylic acid(SA)–mediated defense genes. NPR1 is sequestered in thecytoplasm as an oligomer through intermolecular disulfide bonds.We report that S-nitrosylation of NPR1 by S-nitrosoglutathione(GSNO) at Cys156 facilitates its oligomerization, which maintainsprotein homeostasis upon SA induction. Conversely, the SA-inducedNPR1 oligomer-to-monomer reaction is catalyzed by thioredoxins(TRX). Mutants in both NPR1 Cys156 and TRX compromised NPR1-mediateddisease resistance. Thus, the regulation of NPR1 is throughopposing action of GSNO and TRX. These findings suggest a linkbetween pathogen-triggered redox changes and gene regulationin plant immunity.
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