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Originally published In Press as doi:10.1074/jbc.M002980200 on June 14, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26300-26308, August 25, 2000
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Alternatively Spliced Isoforms of TFII-I
COMPLEX FORMATION, NUCLEAR TRANSLOCATION, AND DIFFERENTIAL GENE REGULATION*

Venugopalan Cheriyath and Ananda L. RoyDagger

From the Department of Pathology and Program in Immunology, Tufts University School of Medicine, Boston, Massachusetts 02111

TFII-I is a multifunctional phosphoprotein with roles in transcription and signal transduction. Here we report characterization of three additional alternatively spliced isoforms of TFII-I. Employing isoform-specific antibodies, we show that the isoforms form a stable complex in vivo preferentially in the nucleus compared with the cytoplasm. We further show that both homomeric and heteromeric interactions are possible and that the heteromeric interactions between a wild type and a nuclear localization-deficient mutant result in nuclear translocation of the complex, leading us to postulate that complex formation might aid in nuclear translocation. In functional assays all four isoforms individually bind to DNA and transactivate reporter genes to a similar extent. However, although co-expression of different TFII-I isoforms leads to enhanced basal activity, it results in attenuated signal responsive activity. Thus, TFII-I might differentially regulate its target genes via complex or subcomplex formation.

* This work is supported by American Cancer Society Grant RPG-98-104-01-TBE (to A. L. R.).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.

Dagger To whom correspondence should be addressed: Dept. of Pathology and Program in Immunology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Tel.: 617-636-6715; Fax: 617-636-2990; E-mail: aroy@opal.tufts.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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