Journal
BIOCHEMICAL JOURNAL
Volume 387, Issue -, Pages 617-626Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20041491
Keywords
acyltransferase; cardiolipin; lysophosphatidylcholine; mitochondria; oil; tafazzin
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When the yeast protein Yprl40w was expressed in Escherichia coli, a lyso-PC [lysophosphatidylcholine (1-acylglycerophos-phorylcholine)] acyltransferase activity was found associated with the membranes of the bacteria. To our knowledge, this is the first identification of a protein capable of cartalysing the acylation of lyso-PC molecules to form PC. Fluorescence microscopy analysis of living yeasts revealed that the fusion protein Ypr140w-green fluorescent protein is targeted to the mitochondria. Moreover, in contrast with wild-type cells, in the absence of acyl-CoA, the yeast mutant deleted for the YPR140w gene has no lyso-PC acyltransferase activity associated with the mitochondrial fraction. When yeast cells were grown in the presence of lactate, the mutant synthesized 2-fold more triacylglycerols when compared with the wild-type. Moreover, its mitochondrial membranes contained a lesser amount of PC and cardiolipin, and the fatty acid composition of these latter was greatly changed. These modifications were accompanied by a 2-fold increase in the respiration rates (states 3 and 4) of the mitochondria. The relationship between the deletion of the YPR140w gene and the lipid composition of the ypr140wA cells is discussed.
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