Three mutations repurpose a plant karrikin receptor to a strigolactone receptor

Uncovering the basis of small-molecule hormone receptors' evolution is paramount to a complete understanding of how protein structure drives function. In plants, hormone receptors for strigolactones are well suited to evolutionary inquiries because closely related homologs have different ligand preferences. More importantly, because of facile plant transgenic systems, receptors can be swapped and quickly assessed functionally in vivo. Here, we show that only three mutations are required to turn the nonstrigolactone receptor, KAI2, into a receptor that recognizes the plant hormone strigolactone. This modified receptor still retains its native function to perceive KAI2 ligands. Our directed evolution studies indicate that only a few keystone mutations are required to increase receptor promiscuity of KAI2, which may have implications for strigolactone receptor evolution in parasitic plants.

Automated summary

This study found that only three mutations are needed to change the ligand preference of the KAI2 receptor, allowing it to recognize strigolactone hormones. The modified receptor still retains it native function to perceive KAI2 ligands. The research indicates that only a few key mutations are required to increase the receptor promiscuity of KAI2.