Plant immunity requires conformational charges of NPR1 via S-nitrosylation and thioredoxins

被引：810

作者：

Tada, Yasuomi ^{[1
]}

Spoel, Steven H. ^{[1
]}

Pajerowska-Mukhtar, Karolina ^{[1
]}

Mou, Zhonglin ^{[1
]}

Song, Junqi ^{[1
]}

Wang, Chun ^{[2
]}

Zuo, Jianru ^{[2
]}

Dong, Xinnian ^{[1
]}

机构：

[1] Duke Univ, Dept Biol, Durham, NC 27708 USA

[2] Chinese Acad Sci, Inst Genet & Dev Biol, Beijing 100101, Peoples R China

来源：

SCIENCE | 2008年 / 321卷 / 5891期

关键词：

D O I：

10.1126/science.1156970

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 cysteine- 156 facilitates its oligomerization, which maintains protein homeostasis upon SA induction. Conversely, the SA- induced NPR1 oligomer- to- monomer reaction is catalyzed by thioredoxins ( TRXs). Mutations in both NPR1 cysteine- 156 and TRX compromised NPR1- mediated disease resistance. Thus, the regulation of NPR1 is through the opposing action of GSNO and TRX. These findings suggest a link between pathogen- triggered redox changes and gene regulation in plant immunity.

引用

页码：952 / 956

页数：5

共 23 条

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