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Updated: May 26, 2026
10:28
Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers
Published on: September 20, 2018
Activator-dependent acetylation of chromatin model systems
Heather J Szerlong1, Jeffrey C Hansen
1Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO, USA.
Methods in Molecular Biology (Clifton, N.J.)
|December 21, 2011
Summary
Histone acetylation, regulated by histone acetyltransferases (HATs), impacts chromatin structure and gene expression. This study uses a novel model to investigate how HATs affect chromatin and transcription by RNA polymerase II.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Eukaryotic gene expression and DNA metabolism are linked to chromatin architecture.
- Gene activation involves histone acetyltransferases (HATs) recruiting to promoters.
- HATs target histone lysine residues in amino-terminal domains (NTDs), influencing chromatin structure.
Purpose of the Study:
- To characterize the impact of targeted histone acetylation on chromatin structure and function.
- To investigate activator-dependent acetylation effects on higher-order chromatin structure and RNA polymerase II transcription.
Main Methods:
- Development of a novel model system using the human T-cell lymphoma virus type 1 promoter.
- Application of a combination of biochemical and biophysical methods.
Main Results:
- Characterization of a novel model system for studying histone acetylation.
- Investigation into the effects of activator-dependent acetylation on chromatin structure.
- Analysis of the impact on RNA polymerase II-mediated transcription.
Conclusions:
- The study provides insights into the functional consequences of histone acetylation on chromatin.
- Findings contribute to understanding gene regulation mechanisms involving chromatin dynamics.
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02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:32Histone 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,...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
02:42Eukaryotic Transcription Activators
Transcription activators are proteins that promote the transcription of genes from DNA to RNA. In most cases, these proteins contain two separate domains ‒ a domain that binds to DNA and a domain for activating transcription; however, in some cases, a single domain is responsible for both binding and activation of transcription, as seen in the glucocorticoid receptor and MyoD.
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These domains are...
The binding domains are capable of recognizing and interacting with regulatory sequences on the DNA. These domains are...
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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
02:25Spreading of Chromatin Modifications
The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
Writers
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Writers
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