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Volume 247, Issue 2 p. 391-395
Full-length article
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Molecular cloning and chromosomal localization of a novel Drosophila protein phosphatase

Viktor Dombrádi

Viktor Dombrádi

MRC Protein Phosphorylation Group, Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, Scotland

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J.Myles Axton

J.Myles Axton

CRC Eukaryotic Molecular Genetics Research Group, Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AZ, England

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David M. Glover

David M. Glover

CRC Eukaryotic Molecular Genetics Research Group, Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AZ, England

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Patricia T.W. Cohen

Corresponding Author

Patricia T.W. Cohen

MRC Protein Phosphorylation Group, Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, Scotland

P.T.W. Cohen, Department of Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, ScotlandSearch for more papers by this author
First published: April 24, 1989
Citations: 30

Abstract

A 1.0 kilobase cDNA coding for the complete amino acid sequence of a putative protein phosphatase (314 amino acid residues, molecular mass 36 kDa) has been isolated from a Drosophila head cDNA library. The cDNA hybridises to a single site on the right arm of the second chromosome at cytological position 55A1–3. The deduced sequence of the protein, designated protein phosphatase-Y, is homologous to the catalytic subunits of Drosophila and rabbit protein phosphatase- 1α (64 and 59% identity, respectively) and rabbit protein phosphatase-2A (39% identity). These and other comparisons demonstrate that this novel enzyme is not the Drosophila counterpart of mammalian protein phosphatases 1, 2A, 2B, 2C or X.