Cloning, sequencing, and expression of the genomic DNA encoding the protein phosphatase cdc25 in Dictyostelium discoideum

A genomic DNA ( Dd-cdc25) encoding the protein phosphatase cdc25 was isolated from the cellular slime mold Dictyostelium discoideum. The Dd-cdc25 DNA sequence, with a length of 2,958 bp, encodes a protein consisting of 986 amino acid (aa) residues. The sequence shares significant identities with cdc...

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Bibliographic Details
Published in:Development genes and evolution 2004-10, Vol.214 (10), p.510-514
Main Authors: Mayanagi, T, Maeda, Y, Hirose, S, Arakane, T, Araki, T, Amagai, A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Blotting, Western
cdc25 Phosphatases - genetics
Cloning, Molecular
Deoxyribonucleic acid
Dictyostelium - genetics
Dictyostelium discoideum
DNA
DNA Primers
Drosophila
Enzymes
Gene Expression
Gene Library
Molecular Sequence Data
Proteins
Reverse Transcriptase Polymerase Chain Reaction
Sequence Alignment
Sequence Analysis, DNA
Xenopus
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Summary:A genomic DNA ( Dd-cdc25) encoding the protein phosphatase cdc25 was isolated from the cellular slime mold Dictyostelium discoideum. The Dd-cdc25 DNA sequence, with a length of 2,958 bp, encodes a protein consisting of 986 amino acid (aa) residues. The sequence shares significant identities with cdc25 from human, mouse, Xenopus, Drosophila, and Shizosaccharomyces pombe, particularly at the C-terminal region including the catalytic site for phosphatase activity. The deduced Dictyostelium cdc25 protein (Dd-cdc25) has the highest molecular mass (109.9 kDa) in several cdc25 species so far reported and contains four regions consisting of unusually long asparagine repeats (22-31) in the sequence. Unexpectedly, however, Western blot analysis using a specific antibody raised against the C terminus (aa 892-986) of Dd-cdc25 demonstrated that the protein exists as a short form (56 kDa), which has the C-terminal active site of phosphatase, during the course of Dictyostelium development. The Western blot analysis also revealed marked changes in the phosphorylated state of the Dd-cdc25, coupling with cellular development.
ISSN:0949-944X
1432-041X
DOI:10.1007/s00427-004-0429-x