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Biochim Biophys Acta. 2010 Apr;1801(4):455-61. doi: 10.1016/j.bbalip.2009.12.005. Epub 2010 Jan 4.

Functional characterization of lysophosphatidic acid phosphatase from Arabidopsis thaliana.

Author information

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

Abstract

Lysophosphatidic acid (LPA) acts as a signaling molecule that regulates diverse cellular processes and it can rapidly be metabolized by phosphatase and acyltransferase. LPA phosphatase gene has not been identified and characterized in plants so far. The BLAST search revealed that the At3g03520 is similar to phospholipase family, and distantly related to bacterial phosphatases. The conserved motif, (J)4XXXNXSFD, was identified in both At3g03520 like phospholipases and acid phosphatases. In silico expression analysis of At3g03520 revealed a high expression during phosphate starvation and abiotic stresses. This gene was overexpressed in Escherichia coli and shown to posses LPA specific phosphatase activity. These results suggest that this gene possibly plays a role in signal transduction and storage lipid synthesis.

PMID:
20045079
DOI:
10.1016/j.bbalip.2009.12.005
[Indexed for MEDLINE]

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