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

Okada, Kazunori; Suzuki, Kengo; Kamiya, Yasuhiro; Zhu, Xiaoli; Fujisaki, Shingo; Nishimura, Yukinobu; Nishino, Tokuzo; Nakagawad, Tsuyoshi; Kawamukai, Makoto; Matsuda, Hideyuki

doi:10.1016/0005-2760(96)00064-1

Cited by 110 publications

(113 citation statements)

References 21 publications

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“…To determine this we measured the adult lifespan of N2 worms fed E. coli engineered to produce Q 7 , Q 8 , Q 9 or Q 10 ( Table 1). The designated Q n isoform is the predominant species in each of these E. coli strains (Okada et al, 1996(Okada et al, , 1997(Okada et al, , 1998Jonassen et al, 2003). In order to determine whether the Q isoforms produced might be altered following the extended incubations required for lifespan determination, we determined the quinone content for each of these E. coli strains recovered from NGM plates following incubation conditions that simulate a lifespan experiment.…”

Section: Diets Containing Q 8 Q 9 Q 10 Isoforms Do Not Influence mentioning

confidence: 99%

Altered bacterial metabolism, not coenzyme Q content, is responsible for the lifespan extension in Caenorhabditis elegans fed an Escherichia coli diet lacking coenzyme Q

et al. 2008

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SummaryCoenzyme Q n is a fully substituted benzoquinone containing a polyisoprene tail of distinct numbers (n) of isoprene groups. Caenorhabditis elegans fed Escherichia coli devoid of Q 8 have a significant lifespan extension when compared to C. elegans fed a standard 'Q-replete' E. coli diet. Here we examine possible mechanisms for the lifespan extension caused by the Q-less E. coli diet. A bioassay for Q uptake shows that a water-soluble formulation of Q 10 is effectively taken up by both clk-1 mutant and wild-type nematodes, but does not reverse lifespan extension mediated by the Q-less E. coli diet, indicating that lifespan extension is not due to the absence of dietary Q per se. The enhanced longevity mediated by the Q-less E. coli diet cannot be attributed to dietary restriction, different Qn isoforms, reduced pathogenesis or slowed growth of the Q-less E. coli , and in fact requires E. coli viability. Q-less E. coli have defects in respiratory metabolism. C. elegans fed Q-replete E. coli mutants with similarly impaired respiratory metabolism due to defects in complex V also show a pronounced lifespan extension, although not as dramatic as those fed the respiratory deficient Q-less E. coli diet. The data suggest that feeding respiratory incompetent E. coli , whether Q-less or Q-replete, produces a robust life extension in wild-type C. elegans . We believe that the fermentation-based metabolism of the E. coli diet is an important parameter of C. elegans longevity.

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Section: Diets Containing Q 8 Q 9 Q 10 Isoforms Do Not Influence mentioning

confidence: 99%

Altered bacterial metabolism, not coenzyme Q content, is responsible for the lifespan extension in Caenorhabditis elegans fed an Escherichia coli diet lacking coenzyme Q

et al. 2008

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“…In yeast, there are eight COQ genes required for Q biosynthesis and mutations or deletions in any of these genes result in the loss of Q production and failure to grow on non-fermentable carbon sources (12). The yeast COQ1 gene encodes a hexaprenyl diphosphate synthase (13) responsible for determining the tail length of Q (14). Coq2p, the polyprenyl diphosphate transferase, then attaches this tail to 4-hydroxybenzoic acid to make 3-hexaprenyl-4-hydroxybenzoic acid (HHB, Fig.…”

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confidence: 99%

Genetic Evidence for a Multi-subunit Complex in Coenzyme Q Biosynthesis in Yeast and the Role of the Coq1 Hexaprenyl Diphosphate Synthase

Gin

Clarke

2005

Journal of Biological Chemistry

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Coenzyme Q (Q) is a lipid that functions as an electron carrier in the mitochondrial respiratory chain in eukaryotes. There are eight complementation groups of Q-deficient Saccharomyces cerevisiae mutants designated coq1-coq8. Here we provide genetic evidence that several of the Coq polypeptides interact with one another. Deletions in any of the COQ genes affect the steady-state expression of Coq3p, Coq4p, and Coq6p. Antibodies that recognize Coq1p, a hexaprenyl diphosphate synthase, were generated and used to determine that Coq1p is peripherally associated with the inner membrane on the matrix side. Yeast ⌬coq1 mutants harboring diverse Coq1 orthologs from prokaryotic species produce distinct sizes of polyprenyl diphosphate and hence distinct isoforms of Q including Q 7 , Q 8 , Q 9 , or Q 10 (Okada, K., Kainou, T., Matsuda, H., and Kawamukai, M. (1998) FEBS Lett. 431, 241-244). We find that steady-state levels of Coq3p, Coq4p, and Coq6p are rescued in some cases to near wild-type levels by the presence of these diverse Coq1 orthologs in the ⌬coq1 mutant. These data suggest that the lipid product of Coq1p or a Q-intermediate derived from polyprenyl diphosphate is involved in stabilizing the Coq3, Coq4, and Coq6 polypeptides.

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“…To further understand the effects of tail length on Q function and transport, we utilized E. coli strains that had been engineered to produce quinones with different tail lengths (17,18). The polyprenyldiphosphate synthase gene ispB was disrupted, and homologues from different organisms were introduced on plasmids, generating E. coli that produced Q 7 , Q 8 , Q 9 , or Q 10 .…”

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confidence: 99%

Reproductive Fitness and Quinone Content of Caenorhabditis elegans clk-1 Mutants Fed Coenzyme Q Isoforms of Varying Length

Jonassen

Davis

Larsen

et al. 2003

Journal of Biological Chemistry

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Caenorhabditis elegans clk-1 mutants lack coenzyme Q 9 and accumulate the biosynthetic intermediate demethoxy-Q 9 . A dietary source of ubiquinone (Q) is required for larval growth and development of the gonad and germ cells. We considered that uptake of the shorter Q 8 isoform present in the Escherichia coli food may contribute to the Clk phenotypes of slowed development and reduced brood size observed when the animals are fed Q-replete E. coli. To test the effect of isoprene tail length, N2 and clk-1 animals were fed E. coli engineered to produce Q 7 , Q 8 , Q 9 , or Q 10 . Wild-type nematodes showed no change in reproductive fitness regardless of the Q n isoform fed. clk-1(e2519) fed the Q 9 diet showed increased egg production; however, this diet did not improve reproductive fitness of the clk-1(qm30) animals. Furthermore, animals with the more severe clk-1(qm30) allele become sterile and their progeny inviable when fed Q 7 -containing bacteria. The content of Q 7 in the mitochondria of clk-1 animals was decreased relative to Q 8 , suggesting less effective transport of Q 7 to the mitochondria, impaired retention, or decreased stability. Additionally, regardless of E. coli diet, clk-1(qm30) animals contain a dysfunctional dense form of mitochondria. The gonads of clk-1(qm30) worms fed Q 7 -containing food were severely shrunken and disordered. The differential fertility of clk-1 mutant nematodes fed Q isoforms may result from changes in Q localization, altered recognition by Q-binding proteins, and/or potential defects in mitochondrial function resulting from the mutant CLK-1 polypeptide itself.

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

Cited by 110 publications

References 21 publications

Altered bacterial metabolism, not coenzyme Q content, is responsible for the lifespan extension in Caenorhabditis elegans fed an Escherichia coli diet lacking coenzyme Q

Altered bacterial metabolism, not coenzyme Q content, is responsible for the lifespan extension in Caenorhabditis elegans fed an Escherichia coli diet lacking coenzyme Q

Genetic Evidence for a Multi-subunit Complex in Coenzyme Q Biosynthesis in Yeast and the Role of the Coq1 Hexaprenyl Diphosphate Synthase

Reproductive Fitness and Quinone Content of Caenorhabditis elegans clk-1 Mutants Fed Coenzyme Q Isoforms of Varying Length

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