[Molecular cloning of Candida albicans phospholipase D].
Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine, a major substrate, to phosphatidic acid and choline, and its activity is regulated by a variety of hormones, growth factors, and other extracellular signals in mammalian cells. Thus, it is now recognized as a signal transducing enzyme such as phosphatidylinositol-specific phospholipase C, adenylate cyclase, or protein tyrosine kinases. Furthermore, recent findings that regulation by members of the ADP-ribosylation factor (ARF) and Rho families of monomeric GTP-binding protein suggest roles of PLD in intracellular vesicle traffi-cking, morphological changes, and mitogenic signaling process. In Saccharomyces cerevisiae, PLD gene has been cloned and revealed to be essential for meiosis. In contrast, little is known about PLD in Candida albicans. As a first step to understand possible physiological roles of PLD in C. albicans, we cloned a PLD gene from a C. albicans genomic DNA library. Deduced amino acid sequence analysis showed the structural similarity to mammalian, yeast, and plant PLDs. It was also suggested employing RT-PCR (reverse transcriptase polymerase chain reaction) that an isozyme of C. albicans PLD was present.
Kanoh
H
H
Department of Dermatology, Gifu University School of Medicine, Tsukasamachi 40, Gifu 500-8705, Japan.
Nakashima
S
S
Kitajima
Y
Y
Nozawa
Y
Y
D002176:Candida albicans / Q000201:enzymology*; D003001:Cloning, Molecular; D010739:Phospholipase D / Q000235:genetics*
D010739:Phospholipase D