Global Insights into the Lysine Acetylome Reveal the Role of Lysine Acetylation in the Adaptation of Bacillus altitudinis to Salt Stress.

Abstract

Bacillus altitudinis is a well-known beneficial microorganism in plant rhizosphere, capable of enhancing plant growth and salt tolerance in saline soils. However, the mechanistic changes underlying salt tolerance in B. altitudinis at the level of post-translational modifications remain unclear. Here, diverse lysine modifications including acetylation, succinylation, crotonylation, and malonylation were determined in the B. altitudinis response to salt stress by immunodetection, and the acetylation level greatly increased under salt stress. The in-depth acetylome landscape showed that 1032 proteins in B. altitudinis were differentially acetylated under salt stress. These proteins were involved in many physiological aspects closely related to salt tolerance like energy generation and conversion, amino acid synthesis and transport, cell motility, signal transduction, secretion system, and repair system. Moreover, we also identified the differential acetylation of key enzymes involved in the major osmolyte biosynthesis and conversion and antioxidant defenses. Thiol peroxidase (TPX), a key protective antioxidant enzyme, had 3 upregulated acetylation sites (K7/139/157) under salt stress. Site-specific mutations demonstrated that K7/139/157 acetylation strongly regulated TPX function in scavenging intracellular ROS, thereby impacting bacterial growth under salt stress. To our knowledge, this is the first study showing that bacteria adaptation to salt stress occurs at the level of PTMs.