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Originally published In Press as doi:10.1074/jbc.M100862200 on January 30, 2001

J. Biol. Chem., Vol. 276, Issue 18, 15264-15268, May 4, 2001
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Positive Regulatory Domain I Binding Factor 1 Silences Class II Transactivator Expression in Multiple Myeloma Cells*

Nilanjan Ghosh, Ildiko Gyory, Gabriela Wright, Justin Wood, and Kenneth L. WrightDagger

From the H. Lee Moffitt Cancer Center, Interdisciplinary Oncology Program and the Department of Biochemistry and Molecular Biology, University of South Florida, Tampa, Florida 33612

The major histocompatibility complex (MHC) class II transactivator (CIITA) acts as a master switch to activate expression of the genes required for MHC-II antigen presentation. During B-cell to plasma cell differentiation, MHC-II expression is actively silenced, but the mechanism has been unknown. In plasma cell tumors such as multiple myeloma the repression of MHC-II is associated with the loss of CIITA. We have identified that positive regulatory domain I binding factor 1 (PRDI-BF1), a transcriptional repressor, inhibits CIITA expression in multiple myeloma cell lines. Repression of CIITA depends on the DNA binding activity of PRDI-BF1 and its specific binding site in the CIITA promoter. Deletion of a histone deacetylase recruitment domain in PRDI-BF1 does not inhibit repression of CIITA nor does blocking histone deacetylase activity. This is in contrast to PRDI-BF1 repression of the c-myc promoter. Repression of CIITA requires either the N-terminal acidic and conserved PR motif or the proline-rich domain. PRDI-BF1 has been shown to be a key regulator of B-cell and macrophage differentiation. These findings now indicate that PRDI-BF1 has at least two mechanisms of repression whose function is dependent on the nature of the target promoter. Importantly, PRDI-BF1 is defined as the key molecule in silencing CIITA and thus MHC-II in multiple myeloma cells.

* This work is supported in part by National Institutes of Health Grant CA80990-R01 and by the Molecular Biology Core Facility at the H. Lee Moffitt Cancer Center. I. G. Y. is supported in part by the Institute of Biomolecular Science, University of South Florida.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: 12902 Magnolia Dr., MRC 4072, H. Lee Moffitt Cancer Center, Tampa, FL 33612. Tel.: 813-979-3918; Fax: 813-979-7264; E-mail: WRIGHTKL@moffitt.usf.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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