title: A different function for a member of an ancient and highly conserved cytochrome P450 family: from essential sterols to plant defense.
abstract: CYP51 sterol demethylases are the only cytochrome P450 enzymes with a conserved function across the animal, fungal, and plant kingdoms (in the synthesis of essential sterols). These highly conserved enzymes, which are important targets for cholesterol-lowering drugs, antifungal agents, and herbicides, are regarded as the most ancient member cytochrome P450 family. Here we present a report of a CYP51 enzyme that has acquired a different function. We show that the plant enzyme AsCYP51H10 is dispensable for synthesis of essential sterols and has been recruited for the production of antimicrobial compounds (avenacins) that confer disease resistance in oats. The AsCyp51H10 gene is synonymous with Sad2, a gene that we previously had defined by mutation as being required for avenacin synthesis. In earlier work, we showed that Sad1, the gene encoding the first committed enzyme in the avenacin pathway (beta-amyrin synthase), had arisen by duplication and divergence of a cycloartenol synthase-like gene. Together these data indicate an intimate evolutionary connection between the sterol and avenacin pathways. Sad1 and Sad2 lie within 70 kb of each other and are expressed specifically in the epidermal cells of the root tip, the site of accumulation of avenacins. These findings raise intriguing questions about the recruitment, coevolution, and regulation of the components of this specialized defense-related metabolic pathway.
authors.affiliation: Department of Metabolic Biology, John Innes Centre, Norwich NR4 7UH, United Kingdom.
authors.forename: Xiaoquan
authors.initials: X
authors.lastname: Qi
authors.forename: Saleha
authors.initials: S
authors.lastname: Bakht
authors.forename: Bo
authors.initials: B
authors.lastname: Qin
authors.forename: Mike
authors.initials: M
authors.lastname: Leggett
authors.forename: Andrew
authors.initials: A
authors.lastname: Hemmings
authors.forename: Fred
authors.initials: F
authors.lastname: Mellon
authors.forename: John
authors.initials: J
authors.lastname: Eagles
authors.forename: Daniele
authors.initials: D
authors.lastname: Werck-Reichhart
authors.forename: Hubert
authors.initials: H
authors.lastname: Schaller
authors.forename: Agnes
authors.initials: A
authors.lastname: Lesot
authors.forename: Rachel
authors.initials: R
authors.lastname: Melton
authors.forename: Anne
authors.initials: A
authors.lastname: Osbourn
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D018554:Avena / Q000201:enzymology* / Q000235:genetics; D017124:Conserved Sequence; D003577:Cytochrome P-450 Enzyme System / Q000502:physiology*; D008969:Molecular Sequence Data; D005810:Multigene Family; D010935:Plant Diseases / Q000235:genetics* / Q000382:microbiology; D012503:Saponins / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D013261:Sterols / Q000378:metabolism*
chemical_list: D012503:Saponins; D013261:Sterols; D003577:Cytochrome P-450 Enzyme System; C091460:avenacin A 1