Abstract Abscisic acid (ABA), a phytohormone that affects key biological processes, is best known for causing stomata closure to protect plants against environmental stresses. The prevailing mechanism for ABA perception is through the PYL/PYR/RCAR family of proteins but reports of other ABA-interacting proteins such as the guard cell outward rectifying K+ channel (GORK), have encouraged the search for more ABA-sensitive proteins. Here, we identified a similar ABA-interacting site as GORK, in an Arabidopsis thaliana ANTHRANILATE SYNTHASE (ASA2). We found that asa2 mutant plants have obvious aberration in ABA-dependent stomata closing. Leaf transcriptomics revealed significantly fewer ABA-induced DEGs in asa2-1 as compared to Col-0. ABA- and other hormone-related terms were also under-represented, indicating an overall reduced genomic sensitivity to ABA. Computational analysis hinted plausible ABA interaction at the predicted site and both indirect and direct in vitro interaction studies showed that ASA2 could interact with ABA in a specific and ligand dependent manner. Importantly, single amino acid substitutions at the ABA site resulted in various degrees of reduced ABA affinities. Further examination of how ABA interaction affects the enzymatic activity of ASA2 and the flow of information in the chloroplast could reveal molecular targets for agrochemical design that will improve plant resilience.
Yu et al. (Tue,) studied this question.