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Summary    Root parasitic plants such as  Striga ,  Orobanche , and  Phelipanche  spp. cause serious damage to crop production world‐wide. Deletion of the  Low Germination Stimulant 1  ( LGS1 ) gene gives a  Striga ‐resistance trait in sorghum ( Sorghum bicolor ). The  LGS1  gene encodes a sulfotransferase‐like protein, but its function has not been elucidated.  Since the profile of strigolactones (SLs) that induce seed germination in root parasitic plants is altered in the  lgs1  mutant, LGS1 is thought to be an SL biosynthetic enzyme. In order to clarify the enzymatic function of LGS1, we looked for candidate SL substrates that accumulate in the  lgs1  mutants and performed  in vivo  and  in vitro  metabolism experiments.  We found the SL precursor 18‐hydroxycarlactonoic acid (18‐OH‐CLA) is a substrate for LGS1. CYP711A cytochrome P450 enzymes (SbMAX1 proteins) in sorghum produce 18‐OH‐CLA. When  LGS1  and  SbMAX1  coding sequences were co‐expressed in  Nicotiana benthamiana  with the upstream SL biosynthesis genes from sorghum, the canonical SLs 5‐deoxystrigol and 4‐deoxyorobanchol were produced.  This finding showed that LGS1 in sorghum uses a sulfo group to catalyze leaving of a hydroxyl group and cyclization of 18‐OH‐CLA. A similar SL biosynthetic pathway has not been found in other plant species.

Strigolactone biosynthesis catalyzed by cytochrome P450 and sulfotransferase in sorghum