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Spreading of Chromatin Modifications

Spreading 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.
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Histone Modification

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.
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Related Experiment Video

Updated: Feb 3, 2026

Generation and Purification of Human INO80 Chromatin Remodeling Complexes and Subcomplexes

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Published on: October 23, 2014

Molecular basis for chromatin assembly and modification by multiprotein complexes.

M Daniel Ricketts^1,2, Joseph Han³, Mary R Szurgot⁴

¹Department of Biochemistry and Biophysics, Perelman School of Medicine at the University of Pennsylvania, Philadelphia, Pennsylvania, 19104.

Protein Science : a Publication of the Protein Society

|October 24, 2018

Summary

This summary is machine-generated.

Recent structural studies reveal how macromolecular complexes regulate chromatin through nucleosome modulation. Histone chaperones and remodelers share common features, impacting histone modification and assembly mechanisms.

Keywords:

Histone chaperones chromatin regulation chromatin remodeling epigenetic mechanisms histone modification complexes histones

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Area of Science:

Molecular Biology
Epigenetics
Structural Biology

Background:

Chromatin landscape regulation relies on nucleosome modulation.
Nucleosomes consist of core histones (H2A, H2B, H3, H4) and DNA.
Histone modification and nucleosome assembly are key epigenetic processes.

Purpose of the Study:

To review recent structural studies on mechanisms of histone modification and nucleosome assembly.
To elucidate how macromolecular complexes interact with histone and nucleosome substrates.
To understand the role of auxiliary subunits in modulating enzymatic activity and specificity.

Main Methods:

Focus on analysis of recent structural studies.
Comparative analysis of histone chaperone and chromatin remodeler complexes.
Examination of structural data to understand subunit interactions and modulations.

Main Results:

Disparate histone chaperones and chromatin remodelers exhibit shared interaction features.
Structural insights reveal mechanisms of nucleosome assembly, spacing, and variant histone incorporation.
Auxiliary subunits significantly influence enzymatic activity and specificity in histone modification complexes.

Conclusions:

Structural biology provides critical insights into epigenetic regulation at the nucleosome level.
Understanding complex interactions is vital for deciphering histone modification and chromatin dynamics.
Further structural analysis will illuminate the precise roles of subunits in epigenetic machinery.