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An Acetyl-Click Chemistry Assay to Measure Histone Acetyltransferase 1 Acetylation
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Quantum-dot-based FRET detection of histone acetyltransferase activity

James E Ghadiali1, Stuart B Lowe, Molly M Stevens

  • 1Department of Materials, Institute for Biomedical Engineering, Imperial College London, Exhibition Road, London, SW7 2AZ UK.

Angewandte Chemie (International Ed. in English)
|March 11, 2011
PubMed
Summary

No abstract available in PubMed .

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Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...

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