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Vol. 12, Issue 4, 997-1007, April 2001
Institut für Biochemie, Technische Universität Graz,
Austria
Three different pathways lead to the synthesis of
phosphatidylethanolamine (PtdEtn) in yeast, one of which is localized
to the inner mitochondrial membrane. To study the contribution of each
of these pathways, we constructed a series of deletion mutants in which
different combinations of the pathways are blocked. Analysis of their
growth phenotypes revealed that a minimal level of PtdEtn is essential
for growth. On fermentable carbon sources such as glucose, endogenous
ethanolaminephosphate provided by sphingolipid catabolism is sufficient
to allow synthesis of the essential amount of PtdEtn through the
cytidyldiphosphate (CDP)-ethanolamine pathway. On nonfermentable carbon
sources, however, a higher level of PtdEtn is required for growth, and
the amounts of PtdEtn produced through the CDP-ethanolamine pathway and
by extramitochondrial phosphatidylserine decarboxylase 2 are not
sufficient to maintain growth unless the action of the former pathway
is enhanced by supplementing the growth medium with ethanolamine. Thus,
in the absence of such supplementation, production of PtdEtn by
mitochondrial phosphatidylserine decarboxylase 1 becomes essential. In
psd1
strains or cho1 strains (defective in phosphatidylserine synthesis), which contain decreased amounts of PtdEtn, the growth rate on nonfermentable carbon sources correlates with the content of PtdEtn in mitochondria, suggesting that
import of PtdEtn into this organelle becomes growth limiting. Although
morphological and biochemical analysis revealed no obvious defects of
PtdEtn-depleted mitochondria, the mutants exhibited an enhanced
formation of respiration-deficient cells. Synthesis of
glycosylphosphatidylinositol-anchored proteins is also impaired in PtdEtn-depleted cells, as demonstrated by delayed maturation of
Gas1p. Carboxypeptidase Y and invertase, on the other hand, were
processed with wild-type kinetics. Thus, PtdEtn depletion does not
affect protein secretion in general, suggesting that high levels of
nonbilayer-forming lipids such as PtdEtn are not essential for membrane
vesicle fusion processes in vivo.
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