MpFAE3, a β-Ketoacyl-CoA Synthase Gene in the LiverwortMarchantia polymorphaL., Is Preferentially Involved in Elongation of Palmitic Acid to Stearic Acid
Author(s) -
Masataka Kajikawa,
Katsuyuki T. Yamato,
Hiroyuki Kanamaru,
Eiji Sakuradani,
Sakayu Shimizu,
Hideya Fukuzawa,
Yasuyoshi Sakai,
Kanji Ohyama
Publication year - 2003
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.67.1667
Subject(s) - marchantia polymorpha , biochemistry , biology , biosynthesis , elongation , atp synthase , fatty acid , fatty acid synthesis , gene , materials science , ultimate tensile strength , metallurgy
Fatty acid chain elongation is a crucial step in the biosynthesis of long chain fatty acids. An essential reaction in the elongation process is condensation of malonyl-CoA with acyl-CoA, which is catalyzed by beta-ketoacyl-CoA synthase (KCS) in plants. We have isolated and characterized the MpFAE3 gene, one of the KCS gene family in the liverwort Marchantia polymorpha. Transgenic M. polymorpha plants overexpressing MpFAE3 accumulate fatty acids 18:0, 20:0, and 22:0. In these plants, the amount of 16:0 is reduced to 50% of wild type. In a heterologous assay, transgenic methylotrophic yeast expressing the MpFAE3 gene accumulates fatty acid 18:0 and generates several longer fatty acids which are not detectable in the control, accompanied by a decrease of 16:0. These observations indicate that the MpFAE3 protein is preferentially involved in the elongation of 16:0 to 18:0 and also in the subsequent steps of 18:0 to 20:0 and 20:0 to 22:0 in M. polymorpha.
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