caa a22 4500 60620833X CHVBK 20210128101022.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s00425-015-2355-8 doi (NATIONALLICENCE)springer-10.1007/s00425-015-2355-8 Biochemical characterization of allene oxide synthases from the liverwort Marchantia polymorpha and green microalgae Klebsormidium flaccidum provides insight into the evolutionary divergence of the plant CYP74 family [Elektronische Daten] [Takao Koeduka, Kimitsune Ishizaki, Cynthia Mwenda, Koichi Hori, Yuko Sasaki-Sekimoto, Hiroyuki Ohta, Takayuki Kohchi, Kenji Matsui] Main conclusion : Allene oxide synthases (AOSs) were isolated from liverworts and charophytes. These AOSs exhibited enzymatic properties similar to those of angiosperms but formed a distinct phylogenetic clade. Allene oxide synthase (AOS) and hydroperoxide lyase (HPL) mediate the formation of precursors of jasmonates and carbon-six volatiles, respectively. AOS and HPL utilize fatty acid hydroperoxides and belong to the plant cytochrome P450 74 (CYP74) family that mediates plant defense against herbivores, pathogens, or abiotic stresses. Although members of the CYP74 family have been reported in mosses and other species, the evolution and function of multiple CYP74 genes in plants remain elusive. Here, we show that the liverwort Marchantia polymorpha belongs to a basal group in the evolution of land plants; has two closely related proteins (59% identity), MpAOS1 and MpAOS2, that are similar to moss PpAOS1 (49 and 47% identity, respectively); and exhibits AOS activity but not HPL activity. We also found that the green microalgae Klebsormidium flaccidum, consist of multicellular and non-branching filaments, contains an enzyme, KfAOS, that is similar to PpAOS1 (37% identity), and converts 13-hydroperoxide of linolenic acid to 12-oxo-phytodienoic acid in a coupled reaction with allene oxide cyclase. Phylogenetic analysis showed two evolutionarily distinct clusters. One cluster comprised AOS and HPL from charophytic algae, liverworts, and mosses, including MpAOSs and KfAOS. The other cluster was formed by angiosperm CYP74. Our results suggest that plant CYP74 enzymes with AOS, HPL, and divinyl ether synthase activities have arisen multiple times and in the two different clades, which occurred prior to the divergence of the flowering plant lineage. Springer-Verlag Berlin Heidelberg, 2015 Allene oxide synthase nationallicence Plant evolution nationallicence CYP74 nationallicence Hydroperoxide lyase nationallicence C8 volatiles nationallicence AOS : Allene oxide synthase nationallicence HPL : Hydroperoxide lyase nationallicence DES : Divinyl ether synthase nationallicence OPDA : 12-Oxo-phytodienoic acid nationallicence 9-HPOD : 9-Hydroperoxy-(E,Z)-10,12-octadecadienoic acid nationallicence 9-HPOT : 9-Hydroperoxy-(E,Z,Z)-10,12,15-octadecatrienoic acid nationallicence 13-HPOD : 13-Hydroperoxy-(E,Z)-9,11-octadecadienoic acid nationallicence 13-HPOT : 13-Hydroperoxy-(E,Z,Z)-9,11,15-octadecatrienoic acid nationallicence 12-HPETE : 12-Hydroperoxy-(Z,Z,E,Z)-5,8,10,14-eicosatetraenoic acid nationallicence 15-HPETE : 15-Hydroperoxy-(Z,Z,Z,E)-5,8,11,13-eicosatetraenoic acid nationallicence 15-HPEPE : 15-Hydroperoxy-(Z,Z,Z,E,Z)-5,8,11,13,17-eicosapentaenoic acid nationallicence HPO : Hydroperoxide nationallicence CYP74 : Cytochrome P450 family 74 nationallicence JA : Jasmonic acid nationallicence JA-Ile : Jasmonic acid-isoleucine nationallicence EST : Expressed sequence tag nationallicence Koeduka Takao Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan aut Ishizaki Kimitsune Graduate School of Science, Kobe University, 657-8501, Kobe, Japan aut Mwenda Cynthia Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, 753-8515, Yamaguchi, Japan aut Hori Koichi Center for Biological Resources and Informatics, Tokyo Institute of Technology, 226-8501, Kanagawa, Japan aut Sasaki-Sekimoto Yuko Earth-Life Science Institute, Tokyo Institute of Technology, 152-8551, Tokyo, Japan aut Ohta Hiroyuki Center for Biological Resources and Informatics, Tokyo Institute of Technology, 226-8501, Kanagawa, Japan aut Kohchi Takayuki Graduate School of Biostudies, Kyoto University, 606-8502, Kyoto, Japan aut Matsui Kenji Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan aut Planta Springer Berlin Heidelberg 242/5(2015-11-01), 1175-1186 0032-0935 242:5<1175 2015 242 425 https://doi.org/10.1007/s00425-015-2355-8 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00425-015-2355-8 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Koeduka Takao Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan aut NATIONALLICENCE 700 1- Ishizaki Kimitsune Graduate School of Science, Kobe University, 657-8501, Kobe, Japan aut NATIONALLICENCE 700 1- Mwenda Cynthia Applied Molecular Bioscience, Graduate School of Medicine, Yamaguchi University, 753-8515, Yamaguchi, Japan aut NATIONALLICENCE 700 1- Hori Koichi Center for Biological Resources and Informatics, Tokyo Institute of Technology, 226-8501, Kanagawa, Japan aut NATIONALLICENCE 700 1- Sasaki-Sekimoto Yuko Earth-Life Science Institute, Tokyo Institute of Technology, 152-8551, Tokyo, Japan aut NATIONALLICENCE 700 1- Ohta Hiroyuki Center for Biological Resources and Informatics, Tokyo Institute of Technology, 226-8501, Kanagawa, Japan aut NATIONALLICENCE 700 1- Kohchi Takayuki Graduate School of Biostudies, Kyoto University, 606-8502, Kyoto, Japan aut NATIONALLICENCE 700 1- Matsui Kenji Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, 753-8515, Yamaguchi, Japan aut NATIONALLICENCE 773 0- Planta Springer Berlin Heidelberg 242/5(2015-11-01), 1175-1186 0032-0935 242:5<1175 2015 242 425