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J. Biol. Chem., Vol. 277, Issue 13, 11156-11164, March 29, 2002
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From the Department of Cell Biology, Albert Einstein College of
Medicine, Bronx, New York 10461
Pax5 (BSAP) is essential for B cell development
and acts both as a transcriptional activator and a repressor. Using a
yeast two-hybrid assay to identify potential coregulators of Pax5, we identified Daxx, a protein that is highly conserved, ubiquitously expressed, and essential for embryonic mouse development. The interaction between Pax5 and Daxx involves the partial homeodomain of
Pax5 and the C-terminal fragment of Daxx. A component of promyelocytic leukemia protein nuclear bodies, Daxx has been implicated in apoptosis and characterized as a transcriptional corepressor. Upon transient transfection assay of Daxx in B cells expressing endogenous Daxx and
Pax5, we observed not only transcriptional corepression but also,
unexpectedly, coactivation in M12.4.1 and A20 mouse B cell lines. Pax5
domains required for coactivation were identified using 293T cells.
Coactivation apparently involves recruitment of the CREB binding
protein (CBP), because we precipitated complexes containing Pax5, Daxx,
and CBP in B cell lines. These data suggest that Daxx can affect
Pax5's roles as an activator or repressor in B cells and describe a
role for Daxx as a transcriptional coactivator.
The Interaction of Pax5 (BSAP) with Daxx Can Result in
Transcriptional Activation in B Cells*
,
*
This work was supported by National Institutes of Health
Grants AI13509 and AI41572 and an Albert Einstein Cancer Center Grant P30 CA13330.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.
Current address: Dept. of Biological Sciences, Long Island
University at Brooklyn, NY 11201.
§
To whom correspondence should be addressed. Tel.: 718-430-2291;
Fax: 718-430-8574; E-mail: birshtei@aecom.yu.edu.
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