Polybromo-1-bromodomains bind histone H3 at specific acetyl-lysine positions

The human polybromo-1 protein is thought to localize the Polybromo, BRG1-associated factors chromatin-remodeling complex to kinetochores during mitosis via direct interaction of its six tandem bromodomains with acetylated nucleosomes. Bromodomains are acetyl-lysine binding modules roughly 100 amino...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-04, Vol.355 (3), p.661-666
Main Authors: Chandrasekaran, Renu, Thompson, Martin
Format: Article
Language:English
Subjects:
Acetyl-lysine
Acetylation
Amino Acid Sequence
Bromodomain
Histone acetylation
Histone code
Histone H3
Histones - chemistry
Histones - metabolism
Humans
Lysine - metabolism
Molecular Sequence Data
Nuclear Proteins - chemistry
Nuclear Proteins - metabolism
Polybromo
Protein Binding
Protein Interaction Mapping
Protein Structure, Tertiary
RNA Cap-Binding Proteins - metabolism
Specificity
Transcription Factors - chemistry
Transcription Factors - metabolism
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Summary:The human polybromo-1 protein is thought to localize the Polybromo, BRG1-associated factors chromatin-remodeling complex to kinetochores during mitosis via direct interaction of its six tandem bromodomains with acetylated nucleosomes. Bromodomains are acetyl-lysine binding modules roughly 100 amino acids in length originally found in chromatin associated proteins. Previous studies verified acetyl-histone binding by each bromodomain, but site-specificity, a central tenet of the histone code hypothesis, was not examined. Here, the acetylation site-dependence of bromodomain–histone interactions was examined using steady-state fluorescence anisotropy. Results indicate that single bromodomains bind specific acetyl-lysine sites within the histone tail with sub-micromolar affinity. Identification of duplicate target sites suggests that native Pb1 interacts with both copies of histone H3 upon nucleosome assembly. Quantitative analysis of single bromodomain–histone interactions can be used to develop hypotheses regarding the histone acetylation pattern that acts as the binding target of the native polybromo-1 protein.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.01.193