AI Article Synopsis

  • - Salicylic acid (SA) is a key hormone for plant immunity, and researchers have identified NPR1 as its direct receptor, which has been a mystery for years.
  • - NPR1 binds to SA through specific cysteine residues (Cys(521) and Cys(529)) and this interaction involves the transition metal copper, influencing how NPR1 activates defense genes.
  • - The binding of SA triggers a structural change in NPR1, allowing it to release a part of itself that was previously inhibiting its activation function, solidifying its role as a critical component in plant defense mechanisms.

Article Abstract

Salicylic acid (SA) is an essential hormone in plant immunity, but its receptor has remained elusive for decades. The transcriptional coregulator NPR1 is central to the activation of SA-dependent defense genes, and we previously found that Cys(521) and Cys(529) of Arabidopsis NPR1's transactivation domain are critical for coactivator function. Here, we demonstrate that NPR1 directly binds SA, but not inactive structural analogs, with an affinity similar to that of other hormone-receptor interactions and consistent with in vivo Arabidopsis SA concentrations. Binding of SA occurs through Cys(521/529) via the transition metal copper. Mechanistically, our results suggest that binding of SA causes a conformational change in NPR1 that is accompanied by the release of the C-terminal transactivation domain from the N-terminal autoinhibitory BTB/POZ domain. While NPR1 is already known as a link between the SA signaling molecule and defense-gene activation, we now show that NPR1 is the receptor for SA.

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Source
http://dx.doi.org/10.1016/j.celrep.2012.05.008DOI Listing

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