The bromodomain: a chromatin-targeting module?

  title={The bromodomain: a chromatin-targeting module?},
  author={Fred Winston and C. David Allis},
  journal={Nature Structural Biology},
It has recently been demonstrated that bromodomains — motifs found in several eukaryotic transcription factors — bind to acetyl-lysine, a modification of histones that is important for transcription. This finding suggests that the regulatory effects of histone acetylation may be exerted by bromodomain-containing proteins. 

Histone deacetylases: silencers for hire.

The MYST family of histone acetyltransferases.

  • R. UtleyJ. Côté
  • Biology, Chemistry
    Current topics in microbiology and immunology
  • 2003
This review sums up the current knowledge on a specific group of proteins that is extremely well conserved throughout evolution, the MYST family of histone acetyltransferases, which play critical roles in various nuclear functions and the control of cell proliferation.

Protein modules that manipulate histone tails for chromatin regulation

It is becoming clear that appropriate coordination of histone modifications and their manipulations by conserved protein modules are integral to gene-specific transcriptional regulation within chromatin.

The Bromodomain Mediates Transcriptional Intermediary Factor 1α-Nucleosome Interactions*

It is proposed that the BrD plays a critical role in vivo by directing transregulators to their cognate location on nucleosomal DNA.

[Histone modification and regulation of chromatin function].

The review briefly describes the nucleosome structure and major modifications of histones and considers the role of such modifications in transcriptional suppression and activation.

Histone modification and regulation of chromatin function

The review briefly describes the nucleosome structure and major modifications of histones and considers the role of such modifications in transcriptional suppression and activation.

Chromatin Remodeling Complexes: The Regulators of Genome Function

Genome in eukaryotes is large enough to be accommodated in tiny nucleus. It is required to achieve high degree of compaction for getting into the nucleus. Compaction is achieved by folding the DNA

Molecular mechanisms of corepressor function.

This chapter discusses some of the unifying features of corepressor complexes that interact with sequence-specific DNA-binding proteins, methyl-CpG- binding proteins, nucleosomal histones, and the basal transcriptional machinery.



Chromatin disruption and modification.

The possible structural basis and functional consequences of the observed alterations in chromatin associated with transcriptional activation and repression are discussed.

Structure and ligand of a histone acetyltransferase bromodomain

The solution structure of the bromodomain of the HAT co-activator P/CAF (p300/CBP-associated factor) reveals an unusual left-handed up-and-down four-helix bundle, and it is shown by a combination of structural and site-directed mutagenesis studies that bromidomains can interact specifically with acetylated lysine, making them the first known protein modules to do so.

The chromo superfamily: new members, duplication of the chromo domain and possible role in delivering transcription regulators to chromatin.

It is hypothesize that the chromo domain may be a vehicle that delivers both positive and negative transcription regulators to the sites of their action on chromatin.

Structure of the chromatin binding (chromo) domain from mouse modifier protein 1

Structural comparisons suggest that chromo domains, of which more than 40 are now known, act as protein interaction motifs and that the MoMOD1 protein acts as an adaptor mediating interactions between different proteins.

The bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4.

A glutathione S-transferase pull down assay is used to show that Gcn5p binds the amino-terminal tails of histones H3 and H4, but not H2A and H2B, and suggests a new structural role for the highly evolutionary conserved bromodomain.

Repression of GCN5 Histone Acetyltransferase Activity via Bromodomain-Mediated Binding and Phosphorylation by the Ku–DNA-Dependent Protein Kinase Complex

It is demonstrated that the catalytic subunit of DNA-PK phosphorylates hGCN5 both in vivo and in vitro and, moreover, that the phosphorylation inhibits the HAT activity of h GCN5.

Alteration of nucleosome structure as a mechanism of transcriptional regulation.

Recently, proteins that were initially identified as necessary for transcriptional regulation have been shown to alter nucleosomal structure and are likely to play a central role in appropriate regulation of eukaryotic genes.