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At4g24160, a Soluble Acyl-Coenzyme A-Dependent Lysophosphatidic Acid Acyltransferase

Ghosh, Ananda K and Chauhan, Neha and Rajakumari, Sona and Daum, Guenther and Rajasekharan, Ram (2009) At4g24160, a Soluble Acyl-Coenzyme A-Dependent Lysophosphatidic Acid Acyltransferase. In: Plant Physiology, 151 (2). pp. 869-881.

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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 alpha/beta-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)(3)HGF, 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.

Item Type: Journal Article
Publication: Plant Physiology
Publisher: American Society of Plant Biologists
Additional Information: Copyright of this article belongs to American Society of Plant Biologists.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 23 Oct 2009 05:31
Last Modified: 19 Sep 2010 05:50
URI: http://eprints.iisc.ac.in/id/eprint/24514

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