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Related Concept Videos

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,...
Spreading of Chromatin Modifications02:25

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...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

Nucleosomes are the DNA-histone complex, where the DNA strand is wound around the histone core. The histone core is an octamer containing two copies of H2A, H2B, H3, and H4 histone proteins.
The paradox
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their main responsibility is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. While on the other hand, they must allow polymerase enzymes to access DNA...

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Related Experiment Video

Updated: May 18, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

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

Enhanced top-down characterization of histone post-translational modifications.

Zhixin Tian, Nikola Tolić, Rui Zhao

    Genome Biology
    |October 5, 2012
    PubMed
    Summary

    A new 2D LC-MS/MS platform efficiently identifies 708 histone isoforms and their post-translational modifications (PTMs) in purified core histones. This method significantly enhances throughput and sensitivity for histone code analysis.

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    Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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    Last Updated: May 18, 2026

    Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
    11:02

    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

    Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry
    05:52

    Histone Modification Screening using Liquid Chromatography, Trapped Ion Mobility Spectrometry, and Time-Of-Flight Mass Spectrometry

    Published on: January 12, 2024

    Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
    08:12

    Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

    Published on: May 5, 2022

    Area of Science:

    • Biochemistry
    • Proteomics
    • Epigenetics

    Background:

    • Core histones undergo post-translational modifications (PTMs) that regulate chromatin structure and function.
    • These PTMs form a 'histone code' interpreted by chromatin-interacting proteins.
    • Accurate characterization of histone PTMs is crucial for understanding epigenetic regulation.

    Purpose of the Study:

    • To develop a novel, high-throughput, and sensitive platform for characterizing histone PTMs.
    • To enable the identification of histone isoforms at the intact protein level.
    • To improve upon traditional methods for comprehensive histone modification analysis.

    Main Methods:

    • Implementation of an online two-dimensional liquid chromatography-tandem mass spectrometry (2D LC-MS/MS) platform.
    • Analysis of purified core histones.
    • Intact protein level characterization of histone isoforms and their PTMs.

    Main Results:

    • Unambiguous identification of 708 distinct histone isoforms from a single analysis.
    • Characterization achieved using only 7.5 µg of purified core histones.
    • Demonstrated significant improvements in throughput and sensitivity compared to existing platforms.

    Conclusions:

    • The developed 2D LC-MS/MS platform offers a powerful tool for high-throughput histone PTM analysis.
    • This platform facilitates a more comprehensive understanding of the histone code.
    • The enhanced sensitivity and throughput advance the field of epigenetics research.