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Papers In Press, published online ahead of print December 17, 2001
Biologia Molecular i Cel·lular, CSIC, Institut de Biologia Molecular de Barcelona, Barcelona 08034
Corresponding Author: jbmbmc{at}ibmb.csic.es
The chromatin High Mobility Group protein 1 (HMGB1)1 is a very abundant and conserved protein that is structured in two HMG-box domains plus a highly acidic C-terminal domain. From the ability to bind DNA unspecifically 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 showed that HMGB1 can recognize several peptide motifs. A computer search of the protein databases found peptide homologies with proteins already known to interact with HMGB1, like p53, and allowed us to identify new potential candidates. Among them, some transcriptional activators like 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 lead us to propose that HMGB1 could play a central role in the stabilization and/or assembly of several multifunctional complexes through protein-protein interactions.
J. Biol. Chem, 10.1074/jbc.M108417200
Submitted on August 31, 2001
Revised on December 7, 2001
Accepted on December 17, 2001
HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences
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