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Originally published In Press as doi:10.1074/jbc.M700397200 on March 29, 2007

J. Biol. Chem., Vol. 282, Issue 21, 15768-15777, May 25, 2007
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REKLES Is an ARID3-restricted Multifunctional Domain*

Dongkyoon Kim, Loren Probst, Chhaya Das, and Philip W. Tucker1

From the Section of Molecular Genetics and Microbiology and Institute of Cell and Molecular Biology, University of Texas, Austin, Texas 78712-0162

Bright/Dril1/ARID3a is a B cell-specific, matrix association (or attachment) region-binding transcriptional regulator of immunoglobulin heavy chain genes and of E2F1-dependent cell cycle progression. Bright contains a central DNA binding domain termed ARID (AT-rich interacting domain) and a C-terminal region termed REKLES (for a conserved amino acid motif). The ARID domain has been identified in seven highly conserved families of metazoan proteins (ARID1-5 and JARID1-2), whereas REKLES is found only in the ARID3 subfamily (composed of Bright/ARID3a, Bdp/ARID3b, and Bright-like/ARID3c). REKLES consists of two subdomains: a modestly conserved N-terminal REKLES{alpha} and a highly conserved (among ARID3 orthologous proteins) C-terminal REKLESbeta. Previously we showed that Bright undergoes nucleocytoplasmic shuttling and that REKLES{alpha} and -beta were required, respectively, for nuclear import and Crm1-dependent nuclear export. Here we show that Bright further requires REKLESbeta for self-association or paralogue association and for nuclear matrix targeting. REK-LES promotes and regulates the extent of Bright multimerization, which occurs in the absence or presence of target DNA and is necessary for specific DNA binding. REKLESbeta-mediated interaction of Bright with Bdp, which localizes strictly to the nucleus, traps Bright within the nucleus via neutralization of its nuclear export activity. These results identify REKLES as a multifunctional domain that has co-evolved with and regulates functional properties of the ARID3 DNA binding domain.


Received for publication, January 16, 2007 , and in revised form, March 23, 2007.

* This work was supported by the National Institutes of Health and the Mary Betzner Morrow Endowment. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 To whom correspondence should be addressed: Molecular Genetics and Microbiology, the University of Texas, 1 University Station A5000, NMS1.124, Austin, TX 78712-0162. Tel.: 512-475-7705; Fax: 512-475-7707; E-mail: philtucker{at}mail.utexas.edu.


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