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The thioesterase APT1 is a bidirectional-adjustment redox sensor
Tuo Ji1, Lihua Zheng1, Jiale Wu1
1State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Nature Communications
|May 17, 2023
Summary
Acyl-protein thioesterase 1 (APT1) acts as a redox sensor, switching between inactive monomeric and active tetrameric forms to manage cellular oxidative stress in plants. This mechanism enhances plant defense against environmental stresses.
Area of Science:
- Plant Biology
- Cellular Biology
- Biochemistry
Background:
- Cellular redox homeostasis is crucial for responding to environmental changes.
- Understanding how cells sense and respond to oxidative states is vital.
Purpose of the Study:
- To identify and characterize acyl-protein thioesterase 1 (APT1) as a novel redox sensor.
- To elucidate the mechanism by which APT1 regulates cellular redox balance in plants.
Main Methods:
- Investigated APT1's oligomeric state (monomer vs. tetramer) under different redox conditions.
- Analyzed APT1's enzymatic activity and substrate interactions (NACsa).
- Assessed downstream effects on gene expression (glyoxalase I) and cellular redox status (GSH/GSSG ratio).
Main Results:
- APT1 functions as a redox sensor, existing as an inactive monomer under normal conditions via S-glutathionylation.
- Oxidative stress triggers APT1 tetramerization, activating its depalmitoylase activity towards NACsa.
- Activated APT1 leads to nuclear translocation of NACsa, increased glutathione levels, and enhanced oxidative stress resistance.
Conclusions:
- APT1 mediates a finely tuned intracellular redox system in plants, crucial for defense against biotic and abiotic stresses.
- The APT1-NACsa pathway offers insights for engineering stress-resistant crops.
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