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Updated: Oct 18, 2025

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
Published on: December 9, 2017
Targeted Protein Acetylation in Cells Using Heterobifunctional Molecules.
Wesley W Wang1, Li-Yun Chen1, Jacob M Wozniak2
1Department of Chemistry, The Scripps Research Institute, Jupiter, Florida 33458, United States.
Researchers developed AceTAG, a novel system for targeted protein acetylation. This tool precisely controls protein acetylation, offering new avenues for biological and therapeutic research.
Area of Science:
- Molecular Biology
- Cellular Biology
- Biochemistry
Background:
- Protein acetylation is crucial for cellular functions but difficult to study with current methods.
- Existing techniques for investigating protein acetylation often lack specificity and control.
Purpose of the Study:
- To develop a novel system, AceTAG, for inducing targeted protein acetylation.
- To provide temporal and magnitude control over protein acetylation in cells.
Main Methods:
- Developed the AceTAG system using bifunctional molecules to recruit p300/CBP to FKBP12-tagged proteins.
- Applied AceTAG to induce acetylation of histone H3.3, p65/RelA, and p53 in cellular models.
Main Results:
- AceTAG successfully induced targeted acetylation of diverse proteins.
- Demonstrated that AceTAG-mediated acetylation is rapid, selective, reversible, and dose-dependent.
Conclusions:
- AceTAG is an effective strategy for modulating protein acetylation.
- This system facilitates the exploration of targeted acetylation in biological and therapeutic research.
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