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Structural analysis of HTL and D14 proteins reveals the basis for ligand selectivity in Striga

Yuqun Xu,T. Miyakawa,Shohei Nosaki,A. Nakamura,Y. Lyu,Hidemitsu Nakamura,U. Ohto,H. Ishida,Toshiyuki Shimizu,T. Asami,M. Tanokura

Published 2018 in Nature Communications

ABSTRACT

HYPOSENSITIVE TO LIGHT (HTL) and DWARF14 (D14) mediate the perception of karrikin and strigolactone, which stimulates germination of the parasitic weed Striga. However, their role in parasitic seeds is poorly understood, and the basis for their differing responsiveness remains unclear. Here, we show that Striga hermonthica HTL proteins (ShHTLs) in ‘conserved’ and ‘intermediate’ clades are able to bind karrikin. The ‘divergent’ clade is able to hydrolyze strigolactone. Unexpectedly, we find that ShD14 is also capable of hydrolyzing strigolactone. Through comparative analysis of ShHTLs and ShD14 crystal structures, we provide insights into the basis for their selectivity. Moreover, we show that both ShD14 and divergent clade ShHTLs, but not conserved and intermediate clade ShHTLs, can interact with the putative downstream signaling component ShMAX2 in the presence of the synthetic strigolactone, rac-GR24. These findings provide insight into how strigolactone is perceived and how ligand specificity is determined. HTL and D14 receptors perceive the structurally similar signaling compounds karrikin and strigolactone. Here, the authors show that ShD14 and a divergent clade of ShHTLs from Strigae capable of recognizing strigolact are capable of recognizing strigolactone and provide structural insights into the evolution of ligand specificity.

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