Molecular cloning of a phospholipase D gene fromAspergillus nidulansand characterization of its deletion mutants

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Abstract
We cloned a gene pldA encoding a protein containing phospholipase D (PLD) motifs from a filamentous fungus Aspergillus nidulans. The deduced protein product of pldA consists of 833 amino acids and contains four conserved regions of a PLD gene family. Deletion mutants of pldA grew and formed conidia in a normal manner. Although PLD and transphosphatidylation activities against phosphatidylcholine of the mutant cell extract did not change, the Ca2+-dependent PLD activity against phosphatidylethanolamine was significantly reduced, but not in the wild-type cell extract. This activity was markedly enhanced by high osmotic growth conditions in the wild-type cells, and pldA of A. nidulans likely encodes a Ca2+-dependent phosphatidylethanolamine-hydrolyzing PLD.