Molecular cloning of a phospholipase D gene from Aspergillus nidulans and characterization of its deletion mutants.
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 Ca(2+)-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 Ca(2+)-dependent phosphatidylethanolamine-hydrolyzing PLD.
Hong
Sahyun
S
Department of Biotechnology, The University of Tokyo, Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.
Horiuchi
Hiroyuki
H
Ohta
Akinori
A
D001233:Aspergillus nidulans / Q000201:enzymology* / Q000235:genetics* / Q000254:growth & development; D002118:Calcium / Q000378:metabolism; D003001:Cloning, Molecular; D003470:Culture Media; D017353:Gene Deletion; D006868:Hydrolysis; D016296:Mutagenesis; D010739:Phospholipase D / Q000235:genetics* / Q000378:metabolism*; D010743:Phospholipids / Q000378:metabolism; D010802:Phylogeny
D003470:Culture Media; D010743:Phospholipids; D010739:Phospholipase D; D002118:Calcium