Functional switching of NPR1 between chloroplast and nucleus for adaptive response to salt stress.

Scientific Reports
So Yeon SeoKy Young Park

Abstract

Salt stress causes rapid accumulation of nonexpressor of pathogenesis-related genes 1 (NPR1) protein, known as the redox-sensitive transcription coactivator, which in turn elicits many adaptive responses. The NPR1 protein transiently accumulates in chloroplast stroma under salt stress, which attenuates stress-triggered down-regulation of photosynthetic capability. We observed that oligomeric NPR1 in chloroplasts and cytoplasm had chaperone activity, whereas monomeric NPR1 in the nucleus did not. Additionally, NPR1 overexpression resulted in reinforcement of morning-phased and evening-phased circadian clock. NPR1 overexpression also enhanced antioxidant activity and reduced stress-induced reactive oxygen species (ROS) generation at early stage, followed with transcription levels for ROS detoxification. These results suggest a functional switch from a molecular chaperone to a transcriptional coactivator, which is dependent on subcellular localization. Our findings imply that dual localization of NPR1 is related to proteostasis and redox homeostasis in chloroplasts for emergency restoration as well as transcriptional coactivator in the nucleus for adaptation to stress.

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Citations

Aug 8, 2021·International Journal of Molecular Sciences·Yasmine S HezemaPraveen K Saxena

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Datasets Mentioned

BETA
ATU76707
KY402167

Methods Mentioned

BETA
protein folding
transgenic
Fluorescence
immunoprecipitation
light scattering
salt stress
environmental stresses
PCR
X-ray

Software Mentioned

Oxyblot
Thermal Cycler Dice ® Real Time System III
ImageJ
Excel

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