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At4g24160, a Soluble Acyl-Coenzyme A-Dependent Lysophosphatidic Acid Acyltransferase
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At4g24160, a Soluble Acyl-Coenzyme A-Dependent Lysophosphatidic Acid Acyltransferase
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Journal Article
At4g24160, a Soluble Acyl-Coenzyme A-Dependent Lysophosphatidic Acid Acyltransferase
2009
Overview
Human CGI-58 (for comparative gene identification-58) and YLR099c, encoding Ict1p in Saccharomyces cerevisiae, have recently been identified as acyl-CoA-dependent lysophosphatidic acid acyltransferases. Sequence database searches for CGI-58 like proteins in Arabidopsis (Arabidopsis thaliana) revealed 24 proteins with At4g24160, a member of the α/β-hydrolase family of proteins being the closest homolog. At4g24160 contains three motifs that are conserved across the plant species: a GXSXG lipase motif, a HX₄D acyltransferase motif, and V(X)₃HGF, a probable lipid binding motif. Dendrogram analysis of yeast ICT1, CGI-58, and At4g24160 placed these three polypeptides in the same group. Here, we describe and characterize At4g24160 as, to our knowledge, the first soluble lysophosphatidic acid acyltransferase in plants. A lipidomics approach revealed that At4g24160 has additional triacylglycerol lipase and phosphatidylcholine hydrolyzing enzymatic activities. These data establish At4g24160, a protein with a previously unknown function, as an enzyme that might play a pivotal role in maintaining the lipid homeostasis in plants by regulating both phospholipid and neutral lipid levels.
Publisher
American Society of Plant Biologists
Subject
/ Acyl Coenzyme A - metabolism
/ Acyltransferases - chemistry
/ Acyltransferases - metabolism
/ Arabidopsis Proteins - chemistry
/ Arabidopsis Proteins - genetics
/ Arabidopsis Proteins - metabolism
/ Biochemical Processes and Macromolecular Structures
/ Biological and medical sciences
/ Butanols
/ Enzymes
/ Fundamental and applied biological sciences. Psychology
/ Gene Expression Regulation, Plant
/ genes
/ genetics
/ Hypoxia
/ Lipids
/ Plant physiology and development
/ proteins
/ Recombinant Proteins - isolation & purification
/ Recombinant Proteins - metabolism
/ Saccharomyces cerevisiae - metabolism
/ Sequence Homology, Amino Acid
/ Solvents
/ Spectrometry, Mass, Electrospray Ionization
/ Subcellular Fractions - enzymology
/ Yeasts
