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J Biol Chem, Vol. 274, Issue 44, 31531-31542, October 29, 1999
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From the To expand our understanding of the role of Jak2
in cellular signaling, we used the yeast two-hybrid system to identify
Jak2-interacting proteins. One of the clones identified represents a
human homologue of the Schizosaccaromyces pombe Shk1
kinase-binding protein 1, Skb1, and the protein encoded by the
Saccharomyces cerevisiae HSL7 (histone synthetic lethal 7)
gene. Since no functional motifs or biochemical activities for this
protein or its homologues had been reported, we sought to determine a
biochemical function for this human protein. We demonstrate that this
protein is a protein methyltransferase. This protein, designated JBP1
(Jak-binding protein 1), and its homologues contain motifs conserved
among protein methyltransferases. JBP1 can be cross-linked to
radiolabeled S-adenosylmethionine (AdoMet) and methylates
histones (H2A and H4) and myelin basic protein. Mutants containing
substitutions within a conserved region likely to be involved in AdoMet
binding exhibit little or no activity. We mapped the JBP1 gene to
chromosome 14q11.2-21. In addition, JBP1 co-immunoprecipitates with
several other proteins, which serve as methyl group acceptors and which may represent physiological targets of this methyltransferase. Messenger RNA for JBP1 is widely expressed in human tissues. We have
also identified and sequenced a homologue of JBP1 in Drosophila melanogaster. This report provides a clue to the biochemical
function for this conserved protein and suggests that protein
methyltransferases may have a role in cellular signaling.
Department of Molecular Genetics and
Microbiology, University of Medicine and Dentistry of New Jersey,
Robert Wood Johnson Medical School, Piscataway, New Jersey 08854-5635 and the § Division of Pediatric Hematology/Oncology,
Children's Regional Hospital at Cooper Hospital/University Medical
Center, Camden, New Jersey 08103
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