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J Biol Chem, Vol. 273, Issue 24, 14933-14941, June 12, 1998
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From the In eukaryotic cells, cardiolipin (CL) synthase
catalyzes the final step in the synthesis of CL from
phosphatidylglycerol and CDP-diacylglycerol. CL and its synthesis are
localized predominantly to the mitochondrial inner membrane, and CL is
generally thought to be an essential component of many mitochondrial
processes. By using homology searches for genes potentially encoding
phospholipid biosynthetic enzymes, we have cloned the gene
(CLS1) encoding CL synthase in Saccharomyces
cerevisiae. Overexpression of the CLS1 gene under its
endogenous promoter or the inducible GAL1 promoter in yeast
and expression of CLS1 in baculovirus-infected insect cells
resulted in elevated CL synthase activity. Disruption of the
CLS1 gene in a haploid yeast strain resulted in the loss of
CL synthase activity, no detectable CL, a 5-fold elevation in
phosphatidylglycerol levels, and lack of staining of mitochondria by a
dye with high affinity for CL. The
cls1::TRP1 null mutant grew on both
fermentable and non-fermentable carbon sources but more poorly on the
latter. The level and activity of cytochrome c oxidase was
normal, and a dye whose accumulation is dependent on membrane proton
electrochemical potential effectively stained the mitochondria. These
results definitively identify the gene encoding the CL synthase of
yeast.
Department of Biochemistry and Molecular
Biology, University of Texas Medical School, Houston, Texas 77225 and
the ¶ National Jewish Center of Immunology and Respiratory
Medicine, Denver, Colorado 80206
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