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J. Biol. Chem., Vol. 275, Issue 26, 19866-19876, June 30, 2000
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From the Arginine methylation is a common post-translation
modification found in many proteins. Protein-arginine methyltransferase I (PRMT1) contributes >90% of type I protein-arginine
methyltransferase activity in cells and tissues. To expand our
knowledge on the regulation and role of PRMT1 in cells, we used the
yeast two-hybrid system to identify proteins that interact with PRMT1.
One of the interacting proteins we cloned is interleukin
enhancer-binding factor 3 (ILF3), also known as M phase phosphoprotein
4. ILF3 is closely related to nuclear factor 90 (NF90). Using an
immunofluorescence analysis, we determined that ILF3 and PRMT1
co-localize in the nucleus. Moreover, PRMT1 and ILF3 co-precipitate in
immunoprecipitation assays and can be isolated together in
"pull-down" experiments using recombinant fusion proteins. ILF3 is
a robust substrate for methylation by PRMT1 and can modulate PRMT1
activity in in vitro methylation assays. Deletion studies
demonstrated that the COOH-terminal region of ILF3, which is rich in
arginine, glycine, and serine, is responsible for the strong
interaction between PRMT1 and ILF3 and is the site of ILF3 methylation
by PRMT1. Although ILF3 and NF90 are highly similar, they differ in
their carboxyl-terminal regions. Because of this difference, NF90 does
not interact with PRMT1, is a much poorer substrate than ILF3 for
PRMT1-dependent methylation, and does not modulate PRMT1
enzyme activity.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF220102.
Protein-arginine Methyltransferase I, the Predominant
Protein-arginine Methyltransferase in Cells, Interacts with and Is
Regulated by Interleukin Enhancer-binding Factor 3*
§¶,
, and§**
Molecular Biology Institute and the
§ Department of Biological Chemistry, UCLA School of
Medicine, Los Angeles, California 90095 and the Division of
Pulmonary and Critical Care Medicine, Stanford University Medical
Center, Stanford, California 94305
*
This work was supported in part by UCLA Asthma, Allergy, and
Immunologic Diseases Center Grant AI34567 from NIAID and NIEHS (to
H. R. H.) and by National Institutes of Health Grant AI39624 (to
P. N. K.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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