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lysophosphatidylcholine/acker schmalwand
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Seite 1 von 28 Ergebnisse
Activation of the plant plasma membrane H+-ATPase. Is there a direct interaction between lysophosphatidylcholine and the C-terminal part of the enzyme?
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The antagonistic effects of the fungal toxin beticolin-1 and of L-alpha-lysophosphatidylcholine (lysoPC) were investigated on the plasma membrane H+-ATPase of the plant Arabidopsis thaliana (isoform 2) expressed in yeast, using both wild-type enzyme (AHA2) and C-terminal truncated enzyme
Expression in yeast of a novel phospholipase A1 cDNA from Arabidopsis thaliana.
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During a search for cDNAs encoding plant sterol acyltransferases, we isolated four full-length cDNAs from Arabidopsis thaliana that encode proteins with substantial identity with animal lecithin : cholesterol acyltransferases (LCATs). The expression of one of these cDNAs, AtLCAT3 (At3g03310), in
A phospholipid uptake system in the model plant Arabidopsis thaliana.
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Plants use solar energy to produce lipids directly from inorganic elements and are not thought to require molecular systems for lipid uptake from the environment. Here we show that Arabidopsis thaliana Aminophospholipid ATPase10 (ALA10) is a P4-type ATPase flippase that internalizes exogenous
Molecular and biochemical characterizations of the monoacylglycerol lipase gene family of Arabidopsis thaliana.
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Monoacylglycerol lipase (MAGL) catalyzes the last step of triacylglycerol breakdown, which is the hydrolysis of monoacylglycerol (MAG) to fatty acid and glycerol. Arabidopsis harbors over 270 genes annotated as 'lipase', the largest class of acyl lipid metabolism genes that have not been
Characterization of two Arabidopsis thaliana acyltransferases with preference for lysophosphatidylethanolamine.
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BACKGROUND
Two previously uncharacterized Arabidopsis genes that encode proteins with acyltransferase PlsC regions were selected for study based on their sequence similarity to a recently identified lung lysophosphatidylcholine acyltransferase (LPCAT). To identify their substrate specificity and
The patatin-containing phospholipase A pPLAIIα modulates oxylipin formation and water loss in Arabidopsis thaliana.
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The patatin-related phospholipase A (pPLA) hydrolyzes membrane glycerolipids to produce monoacyl compounds and free fatty acids. Phospholipids are cleaved by pPLAIIα at the sn-1 and sn-2 positions, and galactolipids, including those containing oxophytodienoic acids, can also serve as substrates.
Rapid kinetic labeling of Arabidopsis cell suspension cultures: implications for models of lipid export from plastids.
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Cell cultures allow rapid kinetic labeling experiments that can provide information on precursor-product relationships and intermediate pools. T-87 suspension cells are increasingly used in Arabidopsis (Arabidopsis thaliana) research, but there are no reports describing their lipid composition or
Calcium and lipid regulation of an Arabidopsis protein kinase expressed in Escherichia coli.
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Calcium-dependent protein kinases (CDPKs) represent a new family of protein kinases which are proposed to contain, in a single polypeptide, both a kinase domain and an adjoining calmodulin-like domain with four calcium-binding EF-hand motifs [Harper, J.F., Sussman, M.R., Schaller, G.E.,
Protein interactors of acyl-CoA-binding protein ACBP2 mediate cadmium tolerance in Arabidopsis.
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In our recent paper in the Plant Journal, we reported that Arabidopsis thaliana lysophospholipase 2 (lysoPL2) binds acyl-CoA-binding protein 2 (ACBP2) to mediate cadmium [Cd(II)] tolerance in transgenic Arabidopsis. ACBP2 contains ankyrin repeats that have been previously shown to mediate
The Arabidopsis sn-1-specific mitochondrial acylhydrolase AtDLAH is positively correlated with seed viability.
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Lipid-derived molecules produced by acylhydrolases play important roles in the regulation of diverse cellular functions in plants. In Arabidopsis, the DAD1-like phospholipase A1 family consists of 12 members, all of which possess a lipase 3 domain. In this study, the biochemical and cellular
On the Role of DGAT1 in Seed Glycerolipid Metabolic Network and Critical Stages of Plant Development in Arabidopsis.
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Studies on the model plant Arabidopsis thaliana have uncovered the identities of most enzymatic components involved in seed storage lipid biosynthesis. However, much remains to be learned on how pathway interactions operate in the seed metabolic network. In this study, we dissected seed glycerolipid
A bifunctional enzyme that has both monoacylglycerol acyltransferase and acyl hydrolase activities.
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Monoacylglycerol acyltransferase (MGAT) catalyzes the synthesis of diacylglycerol, the precursor of triacylglycerol biosynthesis and an important signaling molecule. Here, we describe the isolation and characterization of the peanut (Arachis hypogaea) MGAT gene. The soluble enzyme utilizes invariant
Evidence for Two Catalytic Sites in the Functional Unit of H+-ATPase from Higher Plants.
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We investigated the nature of the complex ATP activation kinetics of plant H+-ATPases. To this aim we analyzed that activation in three isolated isoforms (AHA1, AHA2, and AHA3) of H+-ATPase from Arabidopsis thaliana. The isoforms were obtained by heterologous expression in endoplasmic reticulum of
Metabolically distinct pools of phosphatidylcholine are involved in trafficking of fatty acids out of and into the chloroplast for membrane production.
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The eukaryotic pathway of galactolipid synthesis involves sequential: fatty acid synthesis in the chloroplast; assembly of phosphatidylcholine (PC) in the endoplasmic reticulum (ER); and turnover of PC to provide a substrate for chloroplast galactolipid synthesis. However, the mechanisms and classes
Acyl editing and headgroup exchange are the major mechanisms that direct polyunsaturated fatty acid flux into triacylglycerols.
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Triacylglycerols (TAG) in seeds of Arabidopsis (Arabidopsis thaliana) and many plant species contain large amounts of polyunsaturated fatty acids (PUFA). These PUFA are synthesized on the membrane lipid phosphatidylcholine (PC). However, the exact mechanisms of how fatty acids enter PC and how they
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