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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,...
Histone Variants at the Centromere02:30

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...
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...
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: Jul 6, 2026

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

Proteomic Analysis of Histone Sequence Variants and Post-translationally Modified Forms.

Palina Ryzhaya1,2, Pavlína Pírek1, Radomír Pech1

  • 1Mendel Center for Plant Genomics and Proteomics, Central European Institute of Technology, Masaryk University, Brno, Czech Republic.

Advances in Experimental Medicine and Biology
|July 4, 2026
PubMed
Summary

Histone post-translational modifications (PTMs) are crucial for epigenetic regulation and disease. Mass spectrometry-based proteomics offers advanced methods for comprehensive histone analysis, aiding in understanding gene activity and clinical applications.

Keywords:
Chemical derivatizationHistone characterizationLiquid chromatographyMass spectrometryPost-translational modifications

More Related Videos

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

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Related Experiment Videos

Last Updated: Jul 6, 2026

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

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

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis
07:20

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

Area of Science:

  • Epigenetics and Molecular Biology
  • Proteomics and Mass Spectrometry

Background:

  • Post-translational modifications (PTMs) on histone variants are central to epigenetic regulation, influencing chromatin structure and gene activity.
  • Accurate histone characterization is vital for understanding gene regulation, cellular plasticity, and disease mechanisms.
  • Mass spectrometry coupled with liquid chromatography (LC-MS/MS) is a leading technology for mapping and quantifying histone peptidoforms due to its sensitivity and resolution.

Purpose of the Study:

  • To present key methodologies for comprehensive histone analysis using bottom-up proteomics.
  • To detail protocols for histone extraction, enzymatic digestion, and chemical derivatization for LC-MS/MS.
  • To outline strategies for data evaluation and interpretation in histone proteomics.

Main Methods:

  • Bottom-up proteomics approach for histone analysis.
  • Protocols include histone extraction, enzymatic digestion, and chemical derivatization.
  • Liquid chromatography-tandem mass spectrometry (LC-MS/MS) for high-resolution analysis and data interpretation strategies.

Main Results:

  • Established workflows for detailed mapping and quantification of histone peptidoforms.
  • Demonstrated the analytical challenges posed by histone isoform and PTM diversity.
  • Illustrated the clinical potential of histone proteomics through a case study on male infertility.

Conclusions:

  • Bottom-up proteomics provides essential tools for detailed histone analysis.
  • Standardized workflows are needed for comprehensive and unbiased profiling of histone modifications.
  • Histone proteomics holds significant promise for clinical applications, such as diagnosing male infertility.