Structural dynamics and determinants of abscisic acid-receptor binding preference in different aggregation states.

Abstract

In the 21st century, drought has been the main cause of shortages in world grain production and has created problems with food security. Abscisic acid (ABA) is a key plant hormone involved in the response to abiotic stress, especially drought. The pyrabactin resistance (PYR)/PYR1-like (PYL)/regulatory component of abscisic acid receptor (RCAR) family of proteins (simplified as PYLs) is a well-known ABA receptor family, which can be divided into dimeric and monomeric forms. PYLs can recognize ABA and activate downstream plant drought-resistance signals. However, the difference between monomeric and dimeric receptors in the mechanism of the response to ABA is unclear. Here, we reveal that monomeric receptors have a competitive advantage over dimeric receptors for binding to ABA, driven by the energy penalty resulting from dimer dissociation. ABA also plays different roles with the monomer and the dimer: in the monomer, it acts as a 'conformational stabilizer' for stabilizing the closed gate, whereas for the dimer, it serves as an 'allosteric promoter' for promoting gate closure, which leads to dissociation of the two subunits. This work illustrates how receptor oligomerization could modulate hormonal responses and provides a new concept for novel engineered plants based on ABA binding of monomers.