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Published April 24, 1989 | public
Journal Article

Molecular cloning and chromosomal localization of a novel Drosophila protein phosphatase

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.

Additional Information

© 1989 Federation of European Biochemical Societies. Received 15 March 1989. Thanks are due to Dr D. Kalderon and Professor G.M. Rubin (University of California, Berkeley, CA) for the Drosophila cDNA library, and to Mr A.I.H. Murchie (University of Dundee, Dundee, Scotland) for synthesis of oligonucleotides. This work was supported by a grant from the Wellcome Trust and Group Support from the Medical Research Council, London (to P.T.W.C.) and a grant from the Cancer Research Campaign (to D.M.G.) V.D. was supported by a Long-Term EMBO Fellowship and is on leave from the Institute of Medical Chemistry, University School of Medicine, Debreten, Hungary, J.M.A. holds a Science and Engineering Research Council Studentship. The nucleotide sequence presented here has been submitted to the EMBL/GenBank database under the accession no. YO7510.

Additional details

Created:
August 22, 2023
Modified:
October 20, 2023