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J. Biol. Chem., Vol. 282, Issue 36, 26178-26184, September 7, 2007

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GTP-dependent Recruitment of CIITA to the Class II Major Histocompatibility Complex Promoter^*

Nadine N. Bewry, Sophia C. E. Bolick, Kenneth L. Wright, and Jonathan A. Harton¹

From the Department of Molecular Medicine and the Immunology Program, H. Lee Moffitt Cancer Center, University of South Florida, Tampa, Florida 33612

We previously established that the class II transactivator CIITA binds GTP and disruption of the GTP binding ability of CIITA results in increased cytoplasmic CIITA, loss of nuclear CIITA, and thus diminished class II major histocompatibility complex transcription. Because of its role in facilitating nuclear localization, whether GTP binding is also required for CIITA-mediated transactivation of major histocompatibility class II genes remains unclear. We now show that recruitment of CIITA to the human leukocyte antigen (HLA)-DR promoter and activation of HLA-DR transcription is also GTP-dependent. After restoration of nuclear expression, CIITA mutants defective in GTP binding lack full transcriptional activation capacity. Although the availability of the activation domain of CIITA is unaltered, GTP mutants no longer cooperate with CREB-binding protein, p300, and pCAF and are defective in recruitment to the HLA-DR promoter.

Received for publication, December 22, 2006 , and in revised form, June 12, 2007.

^* This work was supported by American Cancer Society Grant IRG32 (to J. A. H.) and National Institutes of Health Grant K01CA095582 (to J. A. H.). 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: Center for Immunology and Microbial Disease, Albany Medical Center, 47 New Scotland Rd., MC-151, Albany, NY 12208. Tel.: 518-262-4445; Fax: 515-262-6161; E-mail: hartonj{at}mail.amc.edu.

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