Journal
CHEMISTRY & BIOLOGY
Volume 18, Issue 4, Pages 495-507Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2011.02.009
Keywords
-
Categories
Funding
- RIKEN BSI's Research Resources Center for peptide synthesis
- RIKEN BSI-Olympus Collaboration Center
- National Institute of Biomedical Innovation
- RIKEN Structural Genomics/Proteomics Initiative
- MEXT
- Grants-in-Aid for Scientific Research [22790101] Funding Source: KAKEN
Ask authors/readers for more resources
Histone acetylation constitutes an epigenetic mark for transcriptional regulation. Here we developed a fluorescent probe to visualize acetylation of histone H4 Lys12 (H4K12) in living cells using fluorescence resonance energy transfer (FRET) and the binding of the BRD2 bromodomain to acetylated H4K12. Using this probe designated as Histac-K12, we demonstrated that histone H4K12 acetylation is retained in mitosis and that some histone deacetylase (HDAC) inhibitors continue to inhibit cellular HDAC activity even after their removal from the culture. In addition, a small molecule that interferes with ability of the bromodomain to bind to acetylated H4K12 could be assessed using Histac-K12 in cells. Thus, Histac-K12 will serve as a powerful tool not only to understand the dynamics of H4K12-specific acetylation but also to characterize small molecules that modulate the acetylation or interaction status of histones.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available