A Candida albicans homolog of CDC25 is functional in Saccharomyces cerevisiae.
We have cloned, by functional complementation of the cdc25-2 mutation of Saccharomyces cerevisiae, a homolog of CDC25 from the pathogenic yeast Candida albicans. The new gene, named CSC25 codes for a 1333-amino-acid protein. The full length gene, as well as a truncated form coding for 795 amino acids, suppresses the thermosensitive phenotype of cdc25ts mutants. Biochemical analysis has shown that Csc25 activates the Ras/adenylyl cyclase pathway in S. cerevisiae at a rate two to three times faster than Cdc25, under the same conditions. The C-terminal domain of Csc25 is highly similar to the C-terminal domain of Cdc25, to almost the same extent as the C-terminus of the endogenous Cdc25 homolog Sdc25. We show that polyclonal anti-Cdc25 antibodies interact with Csc25 expressed in S. cerevisiae. In addition to the full length protein (approximately 150 kDa), we have found a approximately 50-kDa polypeptide which seems to include the C-terminus of the CSC25 gene product.
Goldberg
D
D
Department of Biological Chemistry, Hebrew University of Jerusalem, Israel.
Marbach
I
I
Gross
E
E
Levitzki
A
A
Simchen
G
G
D000595:Amino Acid Sequence; D001483:Base Sequence; D002176:Candida albicans / Q000235:genetics / Q000378:metabolism*; D018797:Cell Cycle Proteins; D003001:Cloning, Molecular; D004271:DNA, Fungal; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D005947:Glucose / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D020666:ras-GRF1
D018797:Cell Cycle Proteins; D004271:DNA, Fungal; D005656:Fungal Proteins; D020666:ras-GRF1; D005947:Glucose