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At4g24160, a soluble acyl-coenzyme A-dependent lysophosphatidic acid acyltransferase.

Plant Physiol. 2009 Oct;151(2):869-81. Epub 2009 Aug 21
Ananda K Ghosh 1 , Neha Chauhan , Sona Rajakumari , Guenther Daum , Ram Rajasekharan
Ananda K Ghosh 1 , Neha Chauhan , Sona Rajakumari , Guenther Daum , Ram Rajasekharan

[No authors listed]

Author information
  • 1 Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India.

摘要


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 HX(4)D 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.