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Cytochrome b5 diversity in green lineages preceded the evolution of syringyl lignin biosynthesis  ( SCI-EXPANDED收录)  

文献类型:期刊文献

英文题名:Cytochrome b5 diversity in green lineages preceded the evolution of syringyl lignin biosynthesis

作者:Zhao, Xianhai[1] Zhao, Yunjun[1,4] Zeng, Qing-yin[2,3] Liu, Chang-Jun[1]

第一作者:Zhao, Xianhai

通信作者:Liu, CJ[1]

机构:[1]Biol Dept, Brookhaven Natl Lab, Upton, NY 11973 USA;[2]Chinese Acad Forestry, State Key Lab Tree Genet & Breeding, Beijing 100091, Peoples R China;[3]Northeast Forestry Univ, Beijing 100091, Peoples R China;[4]Chinese Acad Sci, Shanghai Inst Plant Physiol & Ecol, CAS Ctr Excellence Mol Plant Sci, 300 Fenglin Rd, Shanghai 200032, Peoples R China

年份:2024

外文期刊名:PLANT CELL

收录:;WOS:【SCI-EXPANDED(收录号:WOS:001220401400001)】;

基金:This work was supported by the U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences under contract number DE-SC0012704-specifically through the Physical Biosciences program of the Chemical Sciences, Geosciences and Biosciences Division (to C.-J.L.). This research used the confocal microscope at the Center for Functional Nanomaterials, which is a U.S. DOE Office of Science Facility, at Brookhaven National Laboratory under contract number DE-SC0012704.

语种:英文

摘要:Lignin production marked a milestone in vascular plant evolution, and the emergence of syringyl (S) lignin is lineage specific. S-lignin biosynthesis in angiosperms, mediated by ferulate 5-hydroxylase (F5H, CYP84A1), has been considered a recent evolutionary event. F5H uniquely requires the cytochrome b5 protein CB5D as an obligatory redox partner for catalysis. However, it remains unclear how CB5D functionality originated and whether it coevolved with F5H. We reveal here the ancient evolution of CB5D-type function supporting F5H-catalyzed S-lignin biosynthesis. CB5D emerged in charophyte algae, the closest relatives of land plants, and is conserved and proliferated in embryophytes, especially in angiosperms, suggesting functional diversification of the CB5 family before terrestrialization. A sequence motif containing acidic amino residues in Helix 5 of the CB5 heme-binding domain contributes to the retention of CB5D function in land plants but not in algae. Notably, CB5s in the S-lignin-producing lycophyte Selaginella lack these residues, resulting in no CB5D-type function. An independently evolved S-lignin biosynthetic F5H (CYP788A1) in Selaginella relies on NADPH-dependent cytochrome P450 reductase as sole redox partner, distinct from angiosperms. These results suggest that angiosperm F5Hs coopted the ancient CB5D, forming a modern cytochrome P450 monooxygenase system for aromatic ring meta-hydroxylation, enabling the reemergence of S-lignin biosynthesis in angiosperms.

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