Open Access
Article
Acetyllysine-binding and function of bromodomain-containing proteins in chromatin
M H Dyson1,S Rose1,L C Mahadevan1
1
Nuclear Signalling Laboratory, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK
DOI: 10.2741/dyson Volume 6 Issue 3, pp.853-865
Published: 01 August 2001
(This article belongs to the Special Issue The role of bromodomain proteins in the cell cycle and cancer)
Abstract

Acetylated histones are generally associated with active chromatin. The bromodomain has recently been identified as a protein module capable of binding to acetylated lysine residues, and hence is able to mediate the recruitment of factors to acetylated chromatin. Functional studies of bromodomain-containing proteins indicate how this domain contributes to the activity of a number of nuclear factors including histone acetyltransferases and chromatin remodelling complexes. Here, we review the characteristics of acetyllysine-binding by bromodomains, discuss associated domains found in these proteins, and address the function of the bromodomain in the context of chromatin. Finally, the modulation of bromodomain binding by neighbouring post-translational modifications within histone tails might provide a mechanism through which combinations of covalent marks could exert control on chromatin function.

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M H Dyson, S Rose, L C Mahadevan. Acetyllysine-binding and function of bromodomain-containing proteins in chromatin. Frontiers in Bioscience-Landmark. 2001. 6(3); 853-865.