Complementation of Escherichia coli ubiF mutation by Caenorhabditis elegans CLK-1, a product of the longevity gene of the nematode worm.
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.
Adachi
Akihiko
A
Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Hongo, Bunkyo-ku, 113-0033, Tokyo, Japan.
Shinjyo
Noriko
N
Fujita
Daisuke
D
Miyoshi
Hideto
H
Amino
Hisako
H
Watanabe
Yoh ichi
Yi
Kita
Kiyoshi
K
D000818:Animals; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000502:physiology*; D004926:Escherichia coli / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D029968:Escherichia coli Proteins; D005816:Genetic Complementation Test; D008136:Longevity; D006899:Mixed Function Oxygenases / Q000235:genetics*; D009154:Mutation; D014451:Ubiquinone / Q000096:biosynthesis
C104339:CLK-1 protein, C elegans; D029742:Caenorhabditis elegans Proteins; D029968:Escherichia coli Proteins; D014451:Ubiquinone; D006899:Mixed Function Oxygenases; C410160:UbiF protein, E coli