Structural basis of salicylic acid perception by Arabidopsis NPR proteins.

ABSTRACT: Salicylic acid (SA) is a plant hormone that is critical for resistance to pathogens^1-3. The NPR proteins have previously been identified as SA receptors^4-10, although how they perceive SA and coordinate hormonal signalling remain unknown. Here we report the mapping of the SA-binding core of Arabidopsis thaliana NPR4 and its ligand-bound crystal structure. The SA-binding core domain of NPR4 refolded with SA adopts an α-helical fold that completely buries SA in its hydrophobic core. The lack of a ligand-entry pathway suggests that SA binding involves a major conformational remodelling of the SA-binding core of NPR4, which we validated using hydrogen-deuterium-exchange mass spectrometry analysis of the full-length protein and through SA-induced disruption of interactions

SUBMITTER: Wang W 

PROVIDER: S-EPMC7554156 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature