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J. Biol. Chem., Vol. 275, Issue 29, 22387-22394, July 21, 2000
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From the Cardiolipin (CL) is a unique phospholipid which
is present throughout the eukaryotic kingdom and is localized in
mitochondrial membranes. Saccharomyces cerevisiae cells
containing a disruption of CRD1, the structural gene
encoding CL synthase, have no CL in mitochondrial membranes. To
elucidate the physiological role of CL, we compared mitochondrial
functions in the crd1
Absence of Cardiolipin in the crd1 Null Mutant
Results in Decreased Mitochondrial Membrane Potential and Reduced
Mitochondrial Function*
§,
,,,
Department of Biological Sciences, Wayne
State University, Detroit, Michigan 48202, the ¶ Institut
für Biochemie und Molekularbiologie, Universität Freiburg,
D-79104 Freiburg, Germany, the Department of Anesthesiology,
Hospital for Special Surgery, New York, New York 10021, and the
** Institut für Physikalische Biochemie, Universität
München, 80336 Munich, Germany
mutant and isogenic wild type. The
crd1 mutant loses viability at elevated temperature, and
prolonged culture at 37 °C leads to loss of the mitochondrial
genome. Mutant membranes have increased phosphatidylglycerol (PG) when
grown in a nonfermentable carbon source but have almost no detectable
PG in medium containing glucose. In glucose-grown cells, maximum
respiratory rate, ATPase and cytochrome oxidase activities, and protein
import are deficient in the mutant. The ADP/ATP carrier is defective
even during growth in a nonfermentable carbon source. The mitochondrial
membrane potential is decreased in mutant cells. The decrease is more
pronounced in glucose-grown cells, which lack PG, but is also apparent
in membranes containing PG (i.e. in nonfermentable carbon
sources). We propose that CL is required for maintaining the
mitochondrial membrane potential and that reduced membrane potential in
the absence of CL leads to defects in protein import and other
mitochondrial functions.
*
This work was supported by a grant from the Deutsche
Forschungsgemeinschaft (to M. K.), grants from the Deutsche
Forschungsgemeinschaft, Sonderforschungsbereich 388 Freiburg and the
Fonds der Chemischen Industrie (to N. P.), and a grant from the
Barbara Ann Karmanos Cancer Institute and National Institutes of Health
Grant HL62263 (to M. G.).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. Tel.: 313-577-5202;
Fax: 313-577-6891; E-mail: MLGREEN@sun.science.wayne.edu.
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