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Actin-endoplasmic reticulum complexes in Drosera: Their structural relationship with the plasmalemma, nucleus, and organelles in cells prepared by high-pressure freezing
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Lichtscheidl I.K., Lancelle S.A., Hepler P.K. Actin-endoplasmic reticulum complexes in Drosera: their structural relationship with the plasmalemma, nucleus, and organelles in cells prepared by high-pressure freezing. Protoplasma. 155:1990;116-126
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Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact
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Achleitner G., Gaigg B., Krasser A., Kainersdorfer E., Kohlwein S.D., Perktold A., Zellnig G., Daum G. Association between the endoplasmic reticulum and mitochondria of yeast facilitates interorganelle transport of phospholipids through membrane contact. Eur J Biochem. 264:1999;545-553
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0038662790
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The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases
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The authors describe a sub-compartment of the ER, termed the MAM, that functions as a bridge between the ER and the mitochondrion and is involved in the biosynthesis and trafficking of phospholipids.
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Ardail D., Popa I., Bobennec J., Louisot P., Schmitt D., Portoukalian J. The mitochondria-associated endoplasmic-reticulum subcompartment (MAM fraction) of rat liver contains highly active sphingolipid-specific glycosyltransferases. Biochem J. 371:2003;1013-1019 The authors describe a sub-compartment of the ER, termed the MAM, that functions as a bridge between the ER and the mitochondrion and is involved in the biosynthesis and trafficking of phospholipids.
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A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids
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Pichler H., Gaigg B., Hrastnik C., Achleitner G., Kohlwein S.D., Zellnig G., Perktold A., Daum G. A subfraction of the yeast endoplasmic reticulum associates with the plasma membrane and has a high capacity to synthesize lipids. Eur J Biochem. 268:2001;2351-2361
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Plastid biogenesis in embryonic pea leaf cells during early germination
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Kaneko Y., Keegstra K. Plastid biogenesis in embryonic pea leaf cells during early germination. Protoplasma. 195:1996;59-67
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Ultrastructural differentiation of plastids and other organelles in rye leaves with a high-temperature-induced deficiency of plastid ribosomes
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Import of lyso-phosphatidylcholine into chloroplasts likely at the origin of eukaryotic plastidial lipids
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Mongrand S., Cassagne C., Bessoule J.J. Import of lyso- phosphatidylcholine into chloroplasts likely at the origin of eukaryotic plastidial lipids. Plant Physiol. 122:2000;845-852
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Transient increase of phosphatidylcholine in plant cells in response to phosphate deprivation
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After exposing plant cell cultures to phosphate deprivation, the authors observed a rapid increase in PC, followed by a decrease that was accompanied by an increase of DGDG with the same molecular profile. At the same time, the content of diacylglycerol rose from 2.5% to 5% of total lipids. These findings strengthen the idea that PC hydrolysis precedes DGDG synthesis. Because the diacylglycerol pool has not been localised, the nature of the lipid moiety that is transported from the ER to the plastid remains unknown.
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Jouhet J., Maréchal E., Bligny R., Joyard J., Block M.A. Transient increase of phosphatidylcholine in plant cells in response to phosphate deprivation. FEBS Lett. 544:2003;63-68 After exposing plant cell cultures to phosphate deprivation, the authors observed a rapid increase in PC, followed by a decrease that was accompanied by an increase of DGDG with the same molecular profile. At the same time, the content of diacylglycerol rose from 2.5% to 5% of total lipids. These findings strengthen the idea that PC hydrolysis precedes DGDG synthesis. Because the diacylglycerol pool has not been localised, the nature of the lipid moiety that is transported from the ER to the plastid remains unknown.
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Fatty acid export from the chloroplast. Molecular characterization of a major plastidial acyl-coenzyme a synthetase from Arabidopsis
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The authors characterise an enzyme that is presumably involved in lipid export from the chloroplast. Long-chain acyl-CoA synthetase9 (LACS9) was localised to the outer chloroplast envelope by chloroplast import studies and by heterologous expression of a green fluorescent protein (GFP) fusion protein. Although the LACS activity of the lacs9 T-DNA knockout mutant was reduced to just 10% of this activity in the wildtype, the growth and lipid composition of this mutant were not affected.
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Schnurr J.A., Shockey J.M., de Boer G.J., Browse J.A. Fatty acid export from the chloroplast. Molecular characterization of a major plastidial acyl-coenzyme A synthetase from Arabidopsis. Plant Physiol. 129:2002;1700-1709 The authors characterise an enzyme that is presumably involved in lipid export from the chloroplast. Long-chain acyl-CoA synthetase9 (LACS9) was localised to the outer chloroplast envelope by chloroplast import studies and by heterologous expression of a green fluorescent protein (GFP) fusion protein. Although the LACS activity of the lacs9 T-DNA knockout mutant was reduced to just 10% of this activity in the wildtype, the growth and lipid composition of this mutant were not affected.
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Schnurr, J.A.1
Shockey, J.M.2
De Boer, G.J.3
Browse, J.A.4
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