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Dimerization through the conserved motif B is involved in chromatin association and function of bromodomain BET proteins

AuthorsGarcía-Gutiérrez, Pablo ; Mundi, María ; García-Domínguez, Mario
Issue Date4-Sep-2012
Citation22nd IUBMB - 37th FEBS Congress (2012)
AbstractBET (Bromodomain and Extra Terminal domain) proteins are unique among bromodomain-containing proteins in that they not only associate to acetylated chromatin in interphase but also remain attached to chromosomes during mitosis. Although the two tandem bromodomains are essential to display this behavior they do not account for full binding capacity. In fact, a deletion construct of the family member Brd2 encompassing just the two bromodomains fails to remain associated to chromosomes in metaphase. By deletion analysis, we have found that a small conserved domain, motif B, is required for that. We also show that motif B-dependent association to chromosomes is not restricted to mitosis, but extends to interphase. Interestingly, our results indicate that the motif B constitutes a coiled-coil surface for homo- and hetero-dimerization between BET proteins. This family of proteins play essential roles in cell cycle progression. Accordingly, we found that dimerization through the motif B is important for Brd2-mediated transactivation of cell cycle genes. Finally, linked to this prominent role in cell proliferation, we observed that ectopic expression of Brd2 interferes with neuronal differentiation in P19 cells and in the vertebrate neural tube, probably due to the maintenance of high levels of cyclins A2 and D1. By contrast, a deletion mutant of the motif B fails to perform in this way, highlighting the relevance of this domain for Brd2 function.
DescriptionPóster presentado al 22nd IUBMB & 37th FEBS Congress: From Single Molecules to Systems Biology, celebrado en Sevilla (España) del 4 al 9 de septiembre de 2012
Appears in Collections:(CABIMER) Comunicaciones congresos
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