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Originally published In Press as doi:10.1074/jbc.M108417200 on December 17, 2001

J. Biol. Chem., Vol. 277, Issue 9, 7021-7028, March 1, 2002
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HMGB1 Interacts with Many Apparently Unrelated Proteins by Recognizing Short Amino Acid Sequences*

Agnès Dintilhac and Jordi BernuésDagger

From the Departament de Biologia Molecular i Cel·lular, Institut de Biologia Molecular de Barcelona, CID, Consell Superior d'Investigacions Científiques, Jordi Girona, 18-26, 08034 Barcelona, Spain

The chromatin high mobility group protein 1 (HMGB1) is a very abundant and conserved protein that is structured into two HMG box domains plus a highly acidic C-terminal domain. From the ability to bind DNA nonspecifically and to interact with various proteins, several functions in DNA-related processes have been assigned to HMGB1. Nevertheless, its functional role remains the subject of controversy. Using a phage display approach we have shown that HMGB1 can recognize several peptide motifs. A computer search of the protein data bases found peptide homologies with proteins already known to interact with HMGB1, like p53, and have allowed us to identify new potential candidates. Among them, transcriptional activators like the heterogeneous nuclear ribonucleoprotein K (hnRNP K), repressors like methyl-CpG binding protein 2 (MeCP2), and co-repressors like the retinoblastoma susceptibility protein (pRb) and Groucho-related gene proteins 1 (Grg1) and 5 (Grg5) can be found. A detailed analysis of the interaction of Grg1 with HMGB1 confirmed that the binding region contained the sequence homologous to one of the peptides identified. Our results have led us to propose that HMGB1 may play a central role in the stabilization and/or assembly of several multifunctional complexes through protein-protein interactions.

* This work was supported by a European Union Grant FMRX-CT97-0109 and Comissió Interdepartamental de Recerca i Innovació Tecnològica (CIRIT) of the Generalitat de Catalunya Grant SGR97-55. This work was carried out in the context of the Centre de Referència en Biotecnologia of the CIRIT of the Generalitat de Catalunya.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: Dept. Biologia Molecular i Cel·lular, Jordi Girona, 18-26, 08034 Barcelona, Spain. Tel.: 34 934 006 177; Fax: 34 932 095 904; E-mail: jbmbmc@ibmb.csic.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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