Evolution of coumaroyl conjugate 3‐hydroxylases in land plants: lignin biosynthesis and defense

• DOI: 10.1111/tpj.14373
• Publication Date: 2019-05-01T02:59:44Z
• Authors: Annette V. Alber; Hugues Renault; Alexandra Basilio...; Jean‐Etienne Bassard; Zhenhua Liu; Pascaline Ullmann; Agnès Lesot; Frédéric Bihel; Martine Schmitt; Danièle Werck‐Rei...; Jürgen Ehlting
• Keywords: Conjugate

Summary Multiple adaptations were necessary when plants conquered the land. Among them soluble phenylpropanoids related to plant protection and lignin for upright growth long‐distance water transport. Cytochrome P450 monooxygenase 98 ( CYP 98) catalyzes a rate‐limiting step in phenylpropanoid biosynthesis. Phylogenetic reconstructions suggest that single copy of founded each major land lineage (bryophytes, lycophytes, monilophytes, gymnosperms angiosperms), was maintained as all lineages but angiosperms. In angiosperms, series independent gene duplications losses occurred. Biochemical assays four angiosperm species tested showed 4‐coumaroyl‐shikimate, known intermediate biosynthesis, preferred substrate one member species, while duplicates Populus trichocarpa Amborella trichopoda broad ranges, accepting numerous 4‐coumaroyl‐esters ‐amines, thus capable producing wide range hydroxycinnamoyl conjugates. The gymnosperm from Pinus taeda range, 4‐coumaroyl‐shikimate its best substrate. contrast, 98s lycophyte Selaginella moellendorffii fern Pteris vittata converted poorly vitro , able use alternative substrates, particular 4‐coumaroyl‐anthranilate. Thus, caffeoyl‐shikimate appears unlikely be an monolignol biosynthesis non‐seed vascular plants, including ferns. 98A34 moss Physcomitrella patens also 4‐coumaroyl‐anthranilate, lower extents. Despite having activity with unable complement Arabidopsis thaliana cyp98a3 loss‐of‐function phenotype, suggesting distinct properties vivo .