Campus Units

Plant Pathology and Microbiology

Document Type

Article

Publication Version

Published Version

Publication Date

12-1-2017

Journal or Book Title

Journal of Biological Chemistry

Volume

292

Issue

48

First Page

19743

Last Page

19751

DOI

10.1074/jbc.M117.803882

Abstract

It is well known that the reactive oxygen species NO can trigger cell death in plants and other organisms, but the underlying molecular mechanisms are not well understood. Here we provide evidence that NO may trigger cell death in tomato (Solanum lycopersicum) by inhibiting the activity of phosphoinositide-dependent kinase 1 (SlPDK1), a conserved negative regulator of cell death in yeasts, mammals, and plants, via S-nitrosylation. Biotin-switch assays indicated that SlPDK1 is a target of S-nitrosylation. Moreover, the kinase activity of SlPDK1 was inhibited by S-nitrosoglutathione in a concentration-dependent manner, indicating that SlPDK1 activity is abrogated by S-nitrosylation. The S-nitrosoglutathione–induced inhibition was reversible in the presence of a reducing agent but additively enhanced by hydrogen peroxide (H2O2). Our LC-MS/MS analyses further indicated that SlPDK1 is primarily S-nitrosylated on a cysteine residue at position 128 (Cys128), and substitution of Cys128 with serine completely abolished SlPDK1 kinase activity, suggesting that S-nitrosylation of Cys128 is responsible for SlPDK1 inhibition. In summary, our results establish a potential link between NO-triggered cell death and inhibition of the kinase activity of tomato PDK1.

Comments

This article is published as Liu, Jian-Zhong, Jicheng Duan, Min Ni, Zhen Liu, Wen-Li Qiu, Steven A. Whitham, and Wei-Jun Qian. "S-Nitrosylation inhibits the kinase activity of tomato phosphoinositide-dependent kinase 1 (PDK1)." Journal of Biological Chemistry 292, no. 48 (2017): 19743-19751. doi:10.1074/jbc.M117.803882.

Creative Commons License

Creative Commons Attribution 4.0 International License
This work is licensed under a Creative Commons Attribution 4.0 International License.

Copyright Owner

ASBMB

Language

en

File Format

application/pdf

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