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A more recent version of this article appeared on December 20, 2002
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Papers In Press, published online ahead of print October 15, 2002
J. Biol. Chem, 10.1074/jbc.M203759200
Submitted on April 18, 2002
Revised on October 15, 2002
Accepted on October 15, 2002

The bromodomain mediates TIF1alpha -nucleosome interactions

Eumorphia Remboutsika, Ken Yamamoto, Matthias Harbers, and Marc Schmutz

Developmental Genetics, National Institute for Medical Research, London NW7 1AA

Corresponding Author: erembou{at}nimr.mrc.ac.uk

Nuclear histone acetyltransferases, DNA-dependent ATPases and transcriptional intermediary factors (TIFs) all harbor a distinct structural module known as the bromodomain (BrD). Although, the BrD can interact with histones H3 and H4 and their acetylated amino-terminal tails in vitro, its function in a chromosomal environment remains elusive. We used the nuclear receptor coregulator TIF1alpha , a protein kinase that associates tightly with euchromatin, to analyze the properties of the BrD in a nucleosomal environment in vitro. Here, we report that TIF1alpha -chromatin association is direct and involves DNA and nucleosome interactions mediated by the BrD. Mutation of the BrD signature peptide, PMDL, abolishes DNA binding and disrupts BrD-nucleosome interactions. Based on our results, we propose that the BrD plays a critical role in vivo by directing transregulators to their cognate location on nucleosomal DNA.


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