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A more recent version of this article appeared on November 9, 2007
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282/45/33009    most recent
M704349200v1
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Papers In Press, published online ahead of print September 11, 2007
J. Biol. Chem, 10.1074/jbc.M704349200
Submitted on May 29, 2007
Revised on August 27, 2007
Accepted on September 10, 2007

Alternative splicing yields protein-arginine methyltransferase 1 isoforms with distinct activity, substrate specificity and subcellular localization

Isabelle Goulet, Gabrielle Gauvin, Sophie Boisvenue, and Jocelyn Cote

Cellular and Molecular Medicine, University of Ottawa, Faculty of Medicine, Ottawa, Ontario K1H 8M5

Corresponding Author: jcote{at}uottawa.ca

PRMT1 is the predominant member of a family of protein arginine methyltransferases (PRMTs) that have been implicated in various cellular processes, including transcription, RNA processing and signal transduction. It was previously reported that the human PRMT1 pre-mRNA was alternatively spliced to yield three isoforms with distinct N-terminal sequences. Close inspection of the genomic organization in the 5’-end of the PRMT1 gene revealed that it can produce up to seven protein isoforms, all varying in their N-terminal domain. A detailed biochemical characterization of these variants revealed that unique N-terminal sequences can influence catalytic activity as well as substrate specificity. In addition, our results uncovered the presence of a functional nuclear export sequence in PRMT1v2. Finally, we find that the relative balance of PRMT1 isoforms is altered in breast cancer.


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J. Sayegh, K. Webb, D. Cheng, M. T. Bedford, and S. G. Clarke
Regulation of Protein Arginine Methyltransferase 8 (PRMT8) Activity by Its N-terminal Domain
J. Biol. Chem., December 14, 2007; 282(50): 36444 - 36453.
[Abstract] [Full Text] [PDF]


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