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J. Biol. Chem., Vol. 280, Issue 30, 27523-27532, July 29, 2005

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High Mobility Group Protein-B1 Interacts with Sterol Regulatory Element-binding Proteins to Enhance Their DNA Binding^*

Yuho Najima, Naoya Yahagi, Yoshinori Takeuchi, Takashi Matsuzaka, Motohiro Sekiya, Yoshimi Nakagawa, Michiyo Amemiya-Kudo, Hiroaki Okazaki, Sachiko Okazaki, Yoshiaki Tamura, Yoko Iizuka, Ken Ohashi, Kenji Harada, Takanari Gotoda, Ryozo Nagai, Takashi Kadowaki, Shun Ishibashi, Nobuhiro Yamada, Jun-ichi Osuga, and Hitoshi Shimano¶

From the Department of Internal Medicine, Graduate School of Medicine, University of Tokyo, Tokyo 113-8655 and the Department of Internal Medicine, Institute of Clinical Medicine, University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8575, Japan

Sterol regulatory element-binding proteins (SREBPs) are transcription factors that are predominately involved in the regulation of lipogenic and cholesterogenic enzyme gene expression. To identify unknown proteins that interact with SREBP, we screened nuclear extract proteins with ³⁵S-labeled SREBP-1 bait in Far Western blotting analysis. Using this approach, high mobility group protein-B1 (HMGB1), a chromosomal protein, was identified as a novel SREBP interacting protein. In vitro glutathione S-transferase pull-down and in vivo coimmunoprecipitation studies confirmed an interaction between HMGB1 and both SREBP-1 and -2. The protein-protein interaction was mediated through the helix-loop-helix domain of SREBP-1, residues 309–344, and the A box of HMGB1. Furthermore, an electrophoretic mobility shift assay demonstrated that HMGB1 enhances SREBPs binding to their cognate DNA sequences. Moreover, luciferase reporter analyses, including RNA interference technique showed that HMGB1 potentiates the transcriptional activities of SREBP in cultured cells. These findings raise the intriguing possibility that HMGB1 is potentially involved in the regulation of lipogenic and cholesterogenic gene transcription.

Received for publication, December 27, 2004 , and in revised form, April 21, 2005.

^* This work was supported by a grant from the Research Fellowships of the Japan Society for the Promotion of Science (to N. Y.). 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.

^¶ To whom correspondence should be addressed. Tel.: 81-29-863-2081; Fax: 81-29-853-3174; E-mail: shimano-tky{at}umin.ac.jp.

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