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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.
Writers
The writer is an enzyme that can...

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.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

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.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...

Histone Variants at the Centromere

Histone Variants at the Centromere

Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3 variants are also...

Inheritance of Chromatin Structures

Inheritance of Chromatin Structures

Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying DNA...

Heterochromatin

Heterochromatin

The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at 9th...

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Related Experiment Video

Updated: May 27, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Barrier-to-Autointegration Factor influences specific histone modifications.

Rocío Montes de Oca¹, Paul R Andreassen, Katherine L Wilson

¹Department of Cell Biology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Nucleus (Austin, Tex.)

|December 1, 2011

Summary

Barrier-to-Autointegration Factor (BAF) is a novel epigenetic regulator. BAF overexpression alters histone modifications, affecting cell cycle and potentially causing diseases like progeria.

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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

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Last Updated: May 27, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Published on: May 17, 2016

Repressing Gene Transcription by Redirecting Cellular Machinery with Chemical Epigenetic Modifiers

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Published on: September 20, 2018

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark

Published on: January 26, 2018

Area of Science:

Cell Biology
Epigenetics
Molecular Biology

Background:

Nuclear envelope and lamina network defects are linked to disease and epigenetic dysregulation.
Barrier-to-Autointegration Factor (BAF) is a key nuclear lamina component with known interactions with lamins, DNA, and histone H3.

Purpose of the Study:

To investigate the role of Barrier-to-Autointegration Factor (BAF) in epigenetic regulation.
To determine how BAF influences histone posttranslational modifications and chromatin states.

Main Methods:

Copurification of BAF with mononucleosomes and assessment of in vivo association with modified histones.
Analysis of global histone acetylation and specific histone mark changes upon BAF overexpression.
Investigation of BAF interactions with key epigenetic modifying enzymes using co-immunoprecipitation.

Main Results:

BAF overexpression significantly reduced global histone H3 acetylation.
Specific silencing and active histone marks were altered, with decreases in H3-K27-Me1/3 and increases in H3-K9-Me3 and H3-K4-Me2.
BAF was found to associate with SET/I2PP2A and G9a, enzymes involved in H3 dephosphorylation and methylation, respectively.

Conclusions:

BAF functions as a novel epigenetic regulator by influencing histone modifications.
Altered histone marks due to BAF dysregulation may contribute to phenotypes observed in BAF deficiency syndromes, including progeria and loss of pluripotency.