Article ID Journal Published Year Pages File Type
9886533 Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 2005 8 Pages PDF
Abstract
The plaA gene encoding a protein that contains the cytosolic Phospholipase A2 (cPLA2) motif is cloned for the first time from the filamentous fungus, Aspergillus nidulans. The translated 837 amino acid protein product of plaA comprises conserved lipase regions that are present in most mammalian cPLA2 homologs. High expression of plaA was observed in glucose-lactose medium by Northern blot analyses. Deletion mutants of plaA grew and formed conidia similar to the wild-type strain, but showed decreased PLA2 activity. Expression of the N-terminal truncated form of plaA in yeast cells resulted in increased Ca2+-dependent PLA2 activity with 14C-labeled phosphatidylcholine (PC) and phosphatidylethanolamine (PE) as substrates, compared with vector-transformed cells. In conclusion, we have identified and cloned a phospholipid-hydrolyzing novel cPLA2 protein from A. nidulans for the first time.
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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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