Polyprenyl diphosphate synthase essentially defines the length of the side chain of ubiquinone

被引:107
作者
Okada, K
Suzuki, K
Kamiya, Y
Zhu, XF
Fujisaki, S
Nishimura, Y
Nishino, T
Nakagawa, T
Kawamukai, M
Matsuda, H
机构
[1] SHIMANE UNIV,FAC LIFE & ENVIRONM SCI,DEPT APPL BIOSCI & BIOTECHNOL,MATSUE,SHIMANE 690,JAPAN
[2] TOHO UNIV,FAC SCI,DEPT BIOMOL SCI,FUNABASHI,CHIBA 274,JAPAN
[3] TOHOKU UNIV,FAC ENGN,DEPT BIOCHEM & ENGN,SENDAI,MIYAGI 98077,JAPAN
[4] SHIMANE UNIV,RES INST MOL GENET,MATSUE,SHIMANE 690,JAPAN
来源
BIOCHIMICA ET BIOPHYSICA ACTA-LIPIDS AND LIPID METABOLISM | 1996年 / 1302卷 / 03期
关键词
ubiquinone; polyprenyl diphosphate synthase; isoprenoid;
D O I
10.1016/0005-2760(96)00064-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ubiquinone, known as a component of the electron transfer system in many organisms, has a different length of the isoprenoid side chain depending on the species, e.g., Escherichia coli, Saccharomyces cerevisiae and humans have 8, 6, and 10 isoprene units in the side chain, respectively. No direct evidence has yet shown what factors define the length of the side chain of ubiquinone. Here we proved that the polyprenyl diphosphate that was available in cells determined the length of the side chain of ubiquinone. E. coli octaprenyl diphosphate synthase (IspB) was expressed with the mitochondrial import signal in S. cerevisiae. Such cells produced ubiquinone-8 in addition to the originally existing ubiquinone-6. When IspB was expressed in a S. cerevisiae COQ1 defective strain, IspB complemented the defect of the growth on the non-fermentable carbon source. Those cells had the activity of octaprenyl diphosphate synthase and produced only ubiquinone-8. These results opened the possibility of producing the type of ubiquinone that we need in S. cerevisiae simply by expressing the corresponding polyprenyl diphosphate synthase.
引用
收藏
页码:217 / 223
页数:7
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