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Updated: Oct 16, 2025

Chromatin Immunoprecipitation ChIP using Drosophila tissue
Published on: March 23, 2012
Interplay Between BALL and CREB Binding Protein Maintains H3K27 Acetylation on Active Genes in Drosophila
Ammad Shaukat1, Muhammad Haider Farooq Khan1, Hina Ahmad1
1Epigenetics and Gene Regulation Laboratory, Department of Biology, Syed Babar Ali School of Science and Engineering, Lahore University of Management Sciences, Lahore, Pakistan.
Insights
The study reveals a new interaction between Ballchen (BALL) and CREB binding protein (CBP) in Drosophila. This synergy is crucial for maintaining gene activation by regulating H3K27ac levels.
Area of Science:
- Molecular Biology
- Genetics
- Epigenetics
Background:
- CREB binding protein (CBP) is a key transcriptional co-activator and histone acetyltransferase.
- CBP-mediated histone H3 lysine 27 acetylation (H3K27ac) marks gene activation by trithorax group proteins (trxG) in Drosophila.
- Ballchen (BALL), a histone kinase, co-localizes with H3K27ac and is essential for maintaining gene activation.
Purpose of the Study:
- To investigate the interaction between BALL and CBP.
- To elucidate the role of this interaction in regulating H3K27ac and gene activation.
Main Methods:
- Genome-wide binding profile analysis of BALL and CBP.
- Biochemical assays to confirm interaction.
- Depletion studies to assess the impact on H3K27ac levels.
Main Results:
- BALL and CBP show significant overlap in genome-wide binding profiles, co-localizing at actively transcribed genes.
- BALL directly interacts with CBP.
- Depletion of BALL leads to a substantial decrease in H3K27ac.
Conclusions:
- A novel synergistic interaction between BALL and CBP has been identified.
- This BALL-CBP pathway plays a critical role in maintaining H3K27ac levels.
- The findings suggest a new mechanism for regulating gene activation during development.
Abstract:
CREB binding protein (CBP) is a multifunctional transcriptional co-activator that interacts with a variety of transcription factors and acts as a histone acetyltransferase. In Drosophila, CBP mediated acetylation of histone H3 lysine 27 (H3K27ac) is a known hallmark of gene activation regulated by trithorax group proteins (trxG). Recently, we have shown that a histone kinase Ballchen (BALL) substantially co-localizes with H3K27ac at trxG target loci and is required to maintain gene activation in Drosophila. Here, we report a previously unknown interaction between BALL and CBP, which positively regulates H3K27ac. Analysis of genome-wide binding profile of BALL and CBP reveals major overlap and their co-localization at actively transcribed genes. We show that BALL biochemically interacts with CBP and depletion of BALL results in drastic reduction in H3K27ac. Together, these results demonstrate a previously unknown synergy between BALL and CBP and reveals a potentially new pathway required to maintain gene activation during development.
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