Specific changes in chromatin structure are associated with transcriptional
regulation. These chromatin alterations include both covalent modification
s of the amino termini of histones as well as ATP-dependent non-covalent re
modeling of nucleosomes. Certain protein domains, such as the bromodomains,
are commonly associated with both of these classes of enzymes that alter c
hromatin. This review discusses recent advances in understanding the struct
ure and function of bromodomains. Most significantly, a role of bromodomain
s has been revealed in binding to acetylated lysine residues in histone tai
ls. Interactions between bromodomains and modified histones may be an impor
tant mechanism underlying chromatin structural changes and gene regulation.
(C) 2001 Elsevier Science B.V. All rights reserved.