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Updated: May 31, 2026
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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
Published on: November 30, 2018
Histone H3 tail acetylation modulates ATP-dependent remodeling through multiple mechanisms
Nilanjana Chatterjee1, Divya Sinha, Mekonnen Lemma-Dechassa
1Department of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901-4413, USA.
Nucleic Acids Research
|July 14, 2011
Summary
Histone H3 acetylation enhances the recruitment and mobilization of chromatin remodelers SWI/SNF and RSC. This bromodomain-dependent process, particularly with H3 acetylation, is crucial for chromatin remodeling and works alongside transcription activators.
Area of Science:
- Molecular Biology
- Epigenetics
- Chromatin Dynamics
Background:
- Histone acetylation and ATP-dependent chromatin remodeling are key epigenetic mechanisms.
- The precise interplay between histone modifications and chromatin remodeler function remains incompletely understood.
Purpose of the Study:
- To investigate how histone H3 acetylation influences the activity of SWI/SNF (mating type switching/sucrose non fermenting) and RSC (remodels structure of chromatin) complexes.
- To elucidate the mechanistic details of how histone acetylation modulates chromatin remodeling.
Main Methods:
- Biochemical assays measuring nucleosome recruitment, mobilization, and ATP hydrolysis.
- Analysis of protein-subunit interactions between chromatin remodelers and histone tails.
- Experiments using tetra-acetylated histone H3 and H4 peptides and nucleosomes.
Main Results:
- Histone H3 acetylation significantly facilitates the recruitment and nucleosome mobilization by SWI/SNF and RSC.
- Tetra-acetylated H3 tails, but not H4, increase the affinity of SWI/SNF and RSC for nucleosomes, dependent on bromodomain interactions.
- H3 acetylation enhances nucleosome mobilization and H2A/H2B displacement in a bromodomain-dependent manner.
- The combined effect of H3 acetylation and transcription activators on SWI/SNF recruitment is synergistic, suggesting parallel pathways.
Conclusions:
- Histone H3 acetylation is a critical regulator of SWI/SNF and RSC activity, enhancing their ability to remodel chromatin.
- Bromodomain interactions are essential for H3 acetylation-mediated enhancement of chromatin remodeler recruitment and function.
- These findings provide mechanistic insights into the coordinated action of histone acetylation and ATP-dependent chromatin remodelers.
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