Structure and function of bromodomains in chromatin-regulating complexes.
Specific changes in chromatin structure are associated with transcriptional regulation. These chromatin alterations include both covalent modifications of the amino termini of histones as well as ATP-dependent non-covalent remodeling of nucleosomes. Certain protein domains, such as the bromodomains, are commonly associated with both of these classes of enzymes that alter chromatin. This review discusses recent advances in understanding the structure and function of bromodomains. Most significantly, a role of bromodomains has been revealed in binding to acetylated lysine residues in histone tails. Interactions between bromodomains and modified histones may be an important mechanism underlying chromatin structural changes and gene regulation.
Marmorstein
R
R
Structural Biology Program, The Wistar Institute, Philadelphia, PA, USA.
Berger
S L
SL
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002843:Chromatin / Q000235:genetics* / Q000378:metabolism; D005786:Gene Expression Regulation; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D002843:Chromatin; D014157:Transcription Factors