[Frontiers in Bioscience 6, d1019-1023, August 1, 2001]

THE BROMODOMAIN: A REGULATOR OF ATP-DEPENDENT CHROMATIN REMODELING?

P.J. Horn, and C.L. Peterson

University of Massachusetts Medical School, Program in Molecular Medicine, 373Plantation St., Worcester, MA 01605

TABLE OF CONTENTS

1. Abstract
2. Introduction
3. The ATP-dependent chromatin remodeling family
4. The bromodomain: A complex regulatory domain?
4.1. Bromodomain function in ATP-dependent chromatin remodeling complexes
4.2. Potential models for bromodomain function
4.2.1. Bromodomains as direct targeting domains
4.2.2. Bromodomains as mediators of complex exchange following recruitment
4.2.3. Bromodomains as allosteric regulators of remodeling complex function
5. Acknowledgements
6. References

1. ABSTRACT

In eukaryotes, processes requiring access to DNA are inhibited by the structural packaging of the genome. A number of specialized ATP-dependent chromatin remodeling enzymes have evolved to overcome this inhibition. One subset of these enzymes, SWI/SNF, plays a critical role in the regulation of transcription, often functioning in concert with nuclear histone acetyltransferases (HATs). It remains unknown how these activities are coordinated. However, recent results revealing that the bromodomain, a motif common in these remodeling factors, constitutes an acetyl-lysine binding domain might provide insight into this process. Bromodomains may serve a role analogous to the signal transduction SH2 domain, by providing a means to recruit remodeling complexes to acetylated chromatin regions or to allosterically modify their function post-recruitment.