14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation
Wendy Walter1, David Clynes, Yong Tang
1Division of Molecular Genetics, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3 QU, United Kingdom.
Molecular and Cellular Biology
|February 13, 2008
Summary
The dual histone modification H3S10phK14ac recruits 14-3-3 proteins, crucial for gene regulation. This interaction requires both phosphorylation and acetylation for optimal binding and transcriptional activation.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Histone modifications regulate gene expression and cell cycle events.
- The dual modification H3S10phK14ac is vital for transcriptional activation.
- The precise mechanism of H3S10phK14ac involvement remains unclear.
Purpose of the Study:
- To identify proteins interacting with the H3S10phK14ac modification.
- To elucidate the role of this dual modification in gene regulation.
Main Methods:
- Utilized H3 peptide affinity assays to identify interacting proteins.
- Investigated the binding of 14-3-3 proteins to H3 with specific modifications.
- Assessed in vivo Bmh1 recruitment to the GAL1 promoter.
Main Results:
- Identified 14-3-3 proteins as interactors with H3S10phK14ac.
- Demonstrated that 14-3-3 binding to H3 requires both serine 10 phosphorylation and lysine 14 acetylation.
- Showed that K14 acetylation is essential for optimal Bmh1 recruitment in vivo.
Conclusions:
- The dual H3S10phK14ac mark is critical for recruiting 14-3-3 proteins.
- This interaction is essential for transcriptional activation.
- Acetylation plays a key role alongside phosphorylation in mediating this interaction.
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