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Published Online July 17, 2008
Science DOI: 10.1126/science.1156970

Reports

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 responses in different organisms, but the associated signaling mechanisms are poorly understood. In plants, these redox changes regulate the conformation of NPR1, a master regulator of salicylic acid (SA)–mediated defense genes. NPR1 is sequestered in the cytoplasm as an oligomer through intermolecular disulfide bonds. We report that S-nitrosylation of NPR1 by S-nitrosoglutathione (GSNO) at Cys156 facilitates its oligomerization, which maintains protein homeostasis upon SA induction. Conversely, the SA-induced NPR1 oligomer-to-monomer reaction is catalyzed by thioredoxins (TRX). Mutants in both NPR1 Cys156 and TRX compromised NPR1-mediated disease resistance. Thus, the regulation of NPR1 is through opposing action of GSNO and TRX. These findings suggest a link between pathogen-triggered redox changes and gene regulation in plant immunity.



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