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Purification of Porcine Brain Protein Phosphatase 2A Leucine Carboxyl Methyltransferase and Cloning of the Human Homologue,

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Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium
Cite this: Biochemistry 1999, 38, 50, 16539–16547
Publication Date (Web):November 19, 1999
Copyright © 1999 American Chemical Society

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    The carboxyl methyltransferase, which is claimed to exclusively methylate the carboxyl group of the C-terminal leucine residue of the catalytic subunit of protein phosphatase 2A (Leu309), was purified from porcine brain. On the basis of tryptic peptides, the cDNA encoding the human homologue was cloned. The cDNA of this gene encodes for a protein of 334 amino acids with a calculated Mr of 38 305 and a predicted pI of 5.72. Database screening reveals the presence of this protein in diverse phyla. Sequence analysis shows that the novel methyltransferase is distinct from other known protein methyltransferases, sharing only sequence motifs supposedly involved in the binding of adenosylmethionine. The recombinant protein expressed in bacteria is soluble and the biophysical, catalytic, and immunological properties are indistinguishable from the native enzyme. The methylation of PP2A by the recombinant protein is restricted to Leu309 of PP2AC. No direct effects on phosphatase activity changes were observed upon methylation of the dimeric or trimeric forms of PP2A.

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     I.D.B. and J.G. are supported by HFSP (Human Frontiers Science Program) and the European Biomed2 program (BMH-CT98-3328). C.V.H. and E.W. are supported by FWO (Fonds Wetenschappelijk Onderzoek Vlaanderen). Financial support was also obtained by grants of GOA (Geconcerteerde OnderzoeksAktie) and IUAP (Inter Universitaire Attractiepool).

     The sequence described in this paper has been submitted to Genbank, Genbank Accession number AF037601.


     Corresponding author:  Dr. Jozef Goris, Afdeling Biochemie, Departement Geneeskunde, Katholieke Universiteit Leuven, Herestraat 49, B-3000 Leuven, Belgium. Telephone:  +32 16 345 794. Fax:  +32 16 345 995. E-mail:  [email protected].

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