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Originally published In Press as doi:10.1074/jbc.C000889200 on January 17, 2001

J. Biol. Chem., Vol. 276, Issue 11, 7713-7716, March 16, 2001
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ACCELERATED PUBLICATION
Altered Quinone Biosynthesis in the Long-lived clk-1 Mutants of Caenorhabditis elegans*

Hiroko MiyaderaDagger , Hisako AminoDagger , Akira Hiraishi§, Hikari Taka, Kimie Murayama, Hideto Miyoshi||, Kimitoshi Sakamoto||, Naoaki Ishii**, Siegfried HekimiDagger Dagger , and Kiyoshi KitaDagger §§

From the Dagger  Department of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan, the § Department of Ecological Engineering, Toyohashi University of Technology, Toyohashi 441-8580, Japan, the  Central Laboratory of Medical Sciences, Juntendo University School of Medicine, Tokyo 113-8421, Japan, the || Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto 606-8502, Japan, the ** Department of Molecular Life Science, Tokai University School of Medicine, Kanagawa 259-1193, Japan, and the Dagger Dagger  Department of Biology, McGill University, Montréal, Québec H3A 1B1, Canada

Mutations in the clk-1 gene of Caenorhabditis elegans result in an extended life span and an average slowing down of developmental and behavioral rates. However, it has not been possible to identify biochemical changes that might underlie the extension of life span observed in clk-1 mutants, and therefore the function of CLK-1 in C. elegans remains unknown. In this report, we analyzed the effect of clk-1 mutation on ubiquinone (UQ9) biosynthesis and show that clk-1 mutants mitochondria do not contain detectable levels of UQ9. Instead, the UQ9 biosynthesis intermediate, demethoxyubiquinone (DMQ9), is present at high levels. This result demonstrates that CLK-1 is absolutely required for the biosynthesis of UQ9 in C. elegans. Interestingly, the activity levels of NADH-cytochrome c reductase and succinate-cytochrome c reductase in mutant mitochondria are very similar to those in the wild-type, suggesting that DMQ9 can function as an electron carrier in the respiratory chain. To test this possibility, the short side chain derivative DMQ2 was chemically synthesized. We find that DMQ2 can act as an electron acceptor for both complex I and complex II in clk-1 mutant mitochondria, while another ubiquinone biosynthesis precursor, 3-hydroxy-UQ2, cannot. The accumulation of DMQ9 and its use in mutant mitochondria indicate, for the first time in any organism, a link between the alteration in the quinone species used in respiration and life span.

* This work was supported by Grant-in-aid for Scientific Research on Priority Areas from the Ministry of Education, Science, Sports and Culture of Japan (No. 11470065) and by the Iwadare Foundation (to H. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§§ To whom correspondence should be addressed: Dept. of Biomedical Chemistry, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan. Tel.: 81-3-5841-3526; Fax: 81-3-5841-3444; E-mail: kitak@m.u-tokyo.ac.jp

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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