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Plant Immunity Requires Conformational Charges of NPR1 via S-Nitrosylation and Thioredoxins
Yasuomi Tada,1
Steven H. Spoel,1
Karolina Pajerowska-Mukhtar,1
Zhonglin Mou,1*
Junqi Song,1
Chun Wang,2
Jianru Zuo,2
Xinnian Dong1
Abstract:
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 cysteine-156 facilitates its oligomerization, whichmaintains protein homeostasis upon SA induction. Conversely,the SA-induced NPR1 oligomer-to-monomer reaction is catalyzedby thioredoxins (TRXs). Mutations in both NPR1 cysteine-156and TRX compromised NPR1-mediated disease resistance. Thus,the regulation of NPR1 is through the opposing action of GSNOand TRX. These findings suggest a link between pathogen-triggeredredox changes and gene regulation in plant immunity.
1 Department of Biology, Post Office Box 90338, Duke University, Durham, NC 27708, USA. 2 Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
* Present address: Department of Microbiology and Cell Science,Post Office Box 110700, University of Florida, Gainesville,FL 32611, USA.
To whom correspondence should be addressed. E-mail: xdong{at}duke.edu
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