GhHSP24.7 mediates mitochondrial protein acetylation to regulate stomatal conductance in response to abiotic stress in cotton

Abstract

During seed germination, the cotton chaperone protein HSP24.7 regulates the release, from the mitochondrial electron transport chain, of reactive oxygen species (ROS), a stimulative signal regulating germination. The function of HSP24.7 during vegetative stages remains largely unknown. Here we propose that suppression of GhHSP24.7 in cotton seedlings increases tolerance to heat and drought stress. Elevation of GhHSP24.7 was found to be positively associated with endogenous levels of ROS. We identified a new client protein of GhHSP24.7, cotton lysine deacetylase (GhHDA14), which is involved in mitochondrial protein modification. Elevated levels of GhHSP24.7 suppressed deacetylase activity in mitochondria, leading to increased acetylation of mitochondrial proteins enriched in the subunit of F-type ATPase, V-type ATPase, and cytochrome C reductase, ultimately reducing leaf ATP content. Consequently, in combination with altered ROS content, GhHSP24.7 transgenic lines were unable to coordinate stomatal closure under stress. The regulation circuit composed of GhHSP24.7 and GhHDA14 represents a post-translation level mechanism in plant abiotic stress responses that integrates the regulation of ROS and ATP.

Keywords

• Heat stress
• Drought stress
• GhHSP24.7
• GhHDA14
• Protein (de)acetylation
• Mitochondria