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Published on: January 26, 2018
Modulating Nucleosomal H3 Tail Dynamics with Lysine and Serine Modifications.
Brandon J Adkins1,2, Paul F W Sidlowski1, Christine E Jennings1
1Department of Biochemistry, Medical College of Wisconsin, Milwaukee, WI, United States.
Biorxiv : the Preprint Server for Biology
|July 10, 2026
Summary
Histone post-translational modifications (PTMs) like acetylation and phosphorylation dynamically alter nucleosome structure. These PTMs increase histone tail flexibility, influencing gene regulation and disease mechanisms.
Area of Science:
- Molecular Biology
- Epigenetics
- Biophysics
Background:
- Nuclear organization relies on dynamic chromatin structure, primarily the nucleosome.
- Histone post-translational modifications (PTMs) regulate chromatin accessibility and gene expression.
- The impact of charge-altering PTMs on histone tail dynamics is not fully understood.
Purpose of the Study:
- To investigate the effects of lysine acetylation and serine phosphorylation on histone H3 tail dynamics.
- To characterize how these PTMs influence nucleosome conformational dynamics.
Main Methods:
- Nuclear magnetic resonance (NMR) spin relaxation experiments were used.
- Lysine-to-glutamine and serine-to-glutamate mutations served as mimetics for acetyllysine and phosphoserine, respectively.
Main Results:
- Acetylation and phosphorylation increase picosecond-nanosecond (ps-ns) conformational dynamics in histone H3 tails.
- The effect of PTMs on dynamics is position-dependent.
- The order of increasing dynamic effect was phosphorylation ≤ acetylation < citrullination.
Conclusions:
- Nucleosome conformational dynamics are crucial for mediating the functional effects of epigenomic PTMs.
- PTMs provide a tunable mechanism for altering histone tail dynamics.
- Understanding these dynamics offers insights into normal cellular function and epigenetic dysregulation in disease.
Related Concept Videos
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,...
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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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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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