1. The structure of protein phosphatase 2A is as highly conserved as that of protein phosphatase I
- Author
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J.Myles Axton, Yadin Dudai, Luke Alphey, Patricia T.W. Cohen, Neil D. Brewis, and Sara Orgad
- Subjects
animal structures ,Phosphatase ,Biophysics ,Biochemistry ,environment and public health ,Amino acid sequence ,Structural Biology ,Complementary DNA ,Drosophilidae ,Genetics ,Molecular Biology ,Peptide sequence ,biology ,Nucleic acid sequence ,Cell Biology ,Protein phosphatase 2 ,biology.organism_classification ,Molecular biology ,Imaginal disc ,Drosophila melanogaster ,Protein phosphatase ,embryonic structures ,Sequence homology ,cDNA cloning ,Nucleotide sequence - Abstract
cDNA coding for protein phosphatase 2A (PP2A) has been isolated from Drosophila head and eye imaginal disc libraries. Drosophila PP2A mRNA is expressed throughout development, but is most abundant in the early embryo. The cDNA hybridises to a single site on the left area of the second chromosomes at position 28D2-4. The deduced amino acid sequence (309 residues) of Drosophila PP2A shows 94% identity with either rabbit PP2Aα or PP2Aβ, indicating that PP2A maybe the most conserved of all known enzymes.
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