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J Biol Chem, Vol. 274, Issue 31, 21665-21672, July 30, 1999
From the Department of Chemistry and Biochemistry and the Molecular
Biology Institute, University of California,
Los Angeles, California 90095
Ubiquinone (coenzyme Q or Q) is a lipid that
functions in the electron transport chain in the inner mitochondrial
membrane of eukaryotes and the plasma membrane of prokaryotes.
Q-deficient mutants of Saccharomyces cerevisiae harbor
defects in one of eight COQ genes (coq1-coq8)
and are unable to grow on nonfermentable carbon sources. The
biosynthesis of Q involves two separate O-methylation steps. In yeast, the first O-methylation utilizes
3,4-dihydroxy-5-hexaprenylbenzoic acid as a substrate and is thought to
be catalyzed by Coq3p, a 32.7-kDa protein that is 40% identical to the
Escherichia coli O-methyltransferase, UbiG. In this study,
farnesylated analogs corresponding to the second
O-methylation step, demethyl-Q3 and Q3, have been chemically synthesized and used to study Q
biosynthesis in yeast mitochondria in vitro. Both yeast and
rat Coq3p recognize the demethyl-Q3 precursor as a
substrate. In addition, E. coli UbiGp was purified and
found to catalyze both O-methylation steps. Futhermore,
antibodies to yeast Coq3p were used to determine that the Coq3
polypeptide is peripherally associated with the matrix-side of the
inner membrane of yeast mitochondria. The results indicate that one
O-methyltransferase catalyzes both steps in Q biosynthesis in eukaryotes and prokaryotes and that Q biosynthesis is carried out
within the matrix compartment of yeast mitochondria.
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