Cloning and characterization of the cpyA gene encoding intracellular carboxypeptidase from Aspergillus nidulans.
Carboxypeptidase Y (CPY) has been used as a maker enzyme for investigations on intracellular transport of vacuolar proteins and on vacuolar biogenesis in Saccharomyces cerevisiae. We describe the cloning and characterization of the CPY homologue encoding gene (cpyA) from the filamentous fungus Aspergillus nidulans. The cpyA gene has one intron and encodes a protein with 552 amino acids containing a putative signal sequence and pro-sequence. The predicted CpyA protein is highly similar in sequence with carboxypeptidases from several yeast species and contains a catalytic triad (Asp-His-Ser) like that of serine carboxypeptidase. The cpyA disruptant cells showed reduced levels of intracellular carboxypeptidase. These results suggest that the cpyA gene encodes a vacuolar carboxypeptidase in A. nidulans.
Ohsumi
K
K
Department of Biotechnology, The University of Tokyo, Japan.
Matsuda
Y
Y
Nakajima
H
H
Kitamoto
K
K
D000595:Amino Acid Sequence; D001233:Aspergillus nidulans / Q000201:enzymology / Q000235:genetics*; D001483:Base Sequence; D002268:Carboxypeptidases / Q000235:genetics* / Q000378:metabolism; D015825:Chromosomes, Fungal; D003001:Cloning, Molecular; D018076:DNA, Complementary; D005800:Genes, Fungal; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D002268:Carboxypeptidases