Structural and functional analyses explain Pea KAI2 receptor diversity and reveal stereoselective catalysis during signal perception

Guercio, Angelica M.; Torabi, Salar; Cornu, David; Dalmais, Marion; Bendahmane, Abdelhafid; Le Signor, Christine; Pillot, Jean-Paul; Le Bris, Philippe; Boyer, François-Didier; Rameau, Catherine; Gutjahr, Caroline; de Saint Germain, Alexandre; Shabek, Nitzan

doi:10.1038/s42003-022-03085-6

Title: Structural and functional analyses explain Pea KAI2 receptor diversity and reveal stereoselective catalysis during signal perception

Journal Article · 10 February 2022 · Communications Biology

DOI: https://doi.org/10.1038/s42003-022-03085-6 · OSTI ID:1903858

^[1]; Torabi, Salar ^[2]; Cornu, David ^[3]; Dalmais, Marion ^[4]; Bendahmane, Abdelhafid ^[4]; Le Signor, Christine ^[5]; Pillot, Jean-Paul ^[6]; Le Bris, Philippe ^[6];

^[3]; Rameau, Catherine ^[6];

^[2];

^[6];

^[7]

University of California, Davis, CA (United States); OSTI
Technical University of Munich (Germany)
University Paris-Saclay, Gif-sur-Yvette (France)
Université Paris-Saclay, Orsay (France)
Université Bourgogne Franche Comte, Dijon (France)
Université Paris-Saclay, Versailles (France)
University of California, Davis, CA (United States)

KAI2 proteins are plant α/β hydrolase receptors which perceive smoke-derived butenolide signals and endogenous, yet unidentified KAI2-ligands (KLs). The number of functional KAI2 receptors varies among species and KAI2 gene duplication and sub-functionalization likely plays an adaptative role by altering specificity towards different KLs. Legumes represent one of the largest families of flowering plants and contain many agronomic crops. Prior to their diversification, KAI2 underwent duplication resulting in KAI2A and KAI2B. Here we demonstrate that Pisum sativum KAI2A and KAI2B are active receptors and enzymes with divergent ligand stereoselectivity. KAI2B has a higher affinity for and hydrolyses a broader range of substrates including strigolactone-like stereoisomers. We determine the crystal structures of PsKAI2B in apo and butenolide-bound states. The biochemical, structural, and mass spectra analyses of KAI2s reveal a transient intermediate on the catalytic serine and a stable adduct on the catalytic histidine, confirming its role as a bona fide enzyme. Our work uncovers the stereoselectivity of ligand perception and catalysis by diverged KAI2 receptors and proposes adaptive sensitivity to KAR/KL and strigolactones by KAI2B.

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Research Organization:: University of California, Davis, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC); National Science Foundation (NSF); CHARM3AT Labex program; Marie-Curie FP7 COFUND; German Research Foundation (DFG); National Institutes of Health (NIH)

Grant/Contract Number:: AC02-05CH11231

OSTI ID:: 1903858

Journal Information:: Communications Biology, Journal Name: Communications Biology Journal Issue: 1 Vol. 5; ISSN 2399-3642

Publisher:: Springer NatureCopyright Statement

Country of Publication:: United States

Language:: English

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Title: Structural and functional analyses explain Pea KAI2 receptor diversity and reveal stereoselective catalysis during signal perception

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