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Related Concept Videos

Histone Modification02:32

Histone Modification

17.4K
The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
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Related Experiment Video

Updated: Apr 11, 2026

Author Spotlight: Developing Acetyl-Click Assay for HAT1 Inhibitor Screening
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A sensitive protein-based sensor for quantifying histone acetylation levels.

Oscar F Sanchez1, Drew Williamson1, Lutong Cai1

  • 1School of Chemical Engineering, Purdue University, 480 Stadium Mall Drive, West Lafayette, IN 47907, USA.

Talanta
|June 7, 2015
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel protein sensor for accurately detecting H3K14ac, a key epigenetic marker. This advancement offers a sensitive and quantitative method for disease monitoring and drug screening.

Keywords:
Histone acetylationHuman polybromo-1Protein sensor

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Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
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Area of Science:

  • Biochemistry
  • Epigenetics
  • Molecular Biology

Background:

  • Histone modifications, such as H3K14ac (acetylation of lysine 14 of histone H3), are crucial epigenetic markers.
  • Aberrant H3K14ac levels are linked to cancers and neurological disorders.
  • Existing detection methods for histone modifications are often labor-intensive and lack quantitative precision.

Purpose of the Study:

  • To engineer a sensitive and quantitative protein sensor for detecting H3K14ac.
  • To optimize detection conditions for improved signal strength and signal-to-noise ratio.
  • To validate the sensor's performance across a range of H3K14ac levels.

Main Methods:

  • Engineered a protein sensor using sequences from the human polybromo-1 (PB1) bromodomain.
  • Conjugated the protein sensor to a fluorescent dye for sensitive detection.
  • Optimized detection parameters (additive and probe concentrations) for signal strength and SNR.
  • Verified the sensor using histone H3 peptides with varying H3K14ac levels.

Main Results:

  • The developed protein sensor demonstrated sensitive detection of H3K14ac.
  • Optimal detection conditions were established by balancing signal intensity and SNR.
  • The sensor exhibited a linear response to H3K14ac levels from 5% to 100%.
  • The platform provides accurate and quantitative measurements of H3K14ac.

Conclusions:

  • A novel, fluorescently labeled protein sensor for H3K14ac detection has been successfully developed.
  • The sensor offers a sensitive, quantitative, and linear detection method for H3K14ac.
  • This platform has potential applications in screening epigenetic drugs and monitoring H3K14ac in circulating nucleosomes for disease progression.