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Originally published In Press as doi:10.1074/jbc.C100346200 on July 2, 2001

J. Biol. Chem., Vol. 276, Issue 36, 33297-33300, September 7, 2001
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ACCELERATED PUBLICATION
A New Member of the Family of Di-iron Carboxylate Proteins
Coq7 (clk-1), A MEMBRANE-BOUND HYDROXYLASE INVOLVED IN UBIQUINONE BIOSYNTHESIS*

Pål Stenmark, Jacob Grünler, Jonas Mattsson, Pavel J. Sindelar, Pär NordlundDagger , and Deborah A. Berthold§

From the Department of Biochemistry and Biophysics, Stockholm University, Svante Arrhenius väg 12, S-106 91 Stockholm, Sweden

Ubiquinone (UQ) is an essential cofactor for respiratory metabolism. In yeast, mutation of the COQ7 gene results in the absence of UQ biosynthesis and demonstrates a role for this gene in the step leading to the hydroxylation of 5-demethoxyubiquinone. Intriguingly, the disruption of the corresponding gene in Caenorhabditis elegans, clk-1, results in a prolonged life span and a slowing of development. Because of the pleiotropic effect of this disruption, the small size of the protein, and the lack of obvious homology to other known hydroxylases, it has been suggested that Coq7 may be a regulatory or structural component in UQ biosynthesis, rather than acting as the hydroxylase per se. Here we identify Coq7 as belonging to a family of a di-iron containing oxidases/hydroxylases based on a conserved sequence motif for the iron ligands, supporting a direct function of Coq7 as a hydroxylase. We have cloned COQ7 from Pseudomonas aeruginosa and Thiobacillus ferrooxidans and show that indeed this gene complements an Escherichia coli mutant that lacks an unrelated 5-demethoxyubiquinone hydroxylase. Based on the similarities to other well studied di-iron carboxylate proteins, we propose a structural model for Coq7 as an interfacial integral membrane protein.

* This work was supported in part by grants from the Swedish Research Council for Natural Sciences and the European Union (EU-TMR Contract Number FMRX-CT98-0207) (to P. N.) and by the Swedish Medical Research Council (to P. J. S.). P. S. was the recipient of a fellowship from the Swedish Foundation for Strategic Research.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.

Dagger To whom correspondence may be addressed. Tel.: 46-8-164141; E-mail: par@dbb.su.se.

§ To whom correspondence may be addressed. Tel.: 46-8-16-2715; Fax: 46-8-15-3679; E-mail: berthold@dbb.su.se.

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


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