Proteome-wide identification of S-sulfenylated cysteines response to salt stress in Brassica napus root

Abstract

Reactive oxygen species (ROS) play a key role in a variety of biological processes, such as the perception of abiotic stress, the integration of different environmental signals, and the activation of stress response networks. Salt stress could induce an increased ROS accumulation in plants, disrupting intracellular redox homeostasis, leading to post-translational modifications (PTMs) of specific proteins, and eventually causing adaptive changes in metabolism. Here, we performed an iodoTMT-based proteomic approach to identify the sulfenylated proteins in B. napus root responsing to salt stress. Totally, 1 348 sulfenylated sites in 751 proteins were identified and these proteins were widely existed in different cell compartments and processes. Our study revealed that proteins with changed abundance and sulfenylation level in B. napus root under salt stress were mainly enriched in the biological processes of ion binding, glycolysis, ATP binding, and oxidative stress response. This study displays a landscape of sulfenylated proteins response to salt stress in B. napus root and provides some theoretical support for further understanding of the molecular mechanisms of redox regulation under salt stress in plants.