Complementation of Escherichia coli ubiF mutation by Caenorhabditis elegans CLK‐1, a product of the longevity gene of the nematode worm

FEBS Letters

Amino, Hisako²  Watanabe, Yoh-ichi²  Fujita, Daisuke¹  Kita, Kiyoshi²  Shinjyo, Noriko²  Miyoshi, Hideto¹  Adachi, Akihiko² 

[1] Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan;Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

关键词: clk-1;    Ubiquinone;    Coq7p;    ubiF;    Hydroxylase;    Caenorhabditis elegans;    Escherichia coli;    DMQ;    demethoxyubiquinone;    DMQ8;    2-octaprenyl-3-methyl-6-methoxy-1;    4-benzoquinone;    ESI;    electrospray ionization;    HPLC;    high-performance liquid chromatography;    PCR;    polymerase chain reaction;    SDS;    sodium dodecyl sulfate;    UQ;    ubiquinone;   

DOI  :  10.1016/S0014-5793(03)00419-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Caenorhabditis elegans CLK-1 was identified from long-lived mutant worms, and is believed to be involved in ubiquinone biosynthesis. The protein belongs to the eukaryotic CLK-1/Coq7p family, which is also similar to the bacterial Coq7 family, that hydroxylates demethoxyubiquinone, resulting in the formation of hydroxyubiquinone, a precursor of ubiquinone. In Escherichia coli, the corresponding reaction is catalyzed by UbiF, a member of a distinct class of hydroxylase. Although previous studies suggested that the eukaryotic CLK-1/Coq7 family is a hydroxylase of demethoxyubiquinone, there was no direct evidence to show the enzymatic activity of the eukaryotic CLK-1/Coq7 family. Here we show that the plasmid encoding C. elegans CLK-1 supported aerobic respiration on a non-fermentable carbon source of E. coli ubiF mutant strain and rescued the ability to synthesize ubiquinone, suggesting that the eukaryotic CLK-1/Coq7p family could function as bacterial UbiF.

【 授权许可】

Unknown