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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...
Inheritance of Chromatin Structures03:17

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...
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...

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Related Experiment Video

Updated: Jun 25, 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 modifications dictate specific biological readouts.

Anjana Munshi1, Gowhar Shafi, Nishat Aliya

  • 1Institute of Genetics and Hospital for Genetic Diseases, Begumpet, Hyderabad, India. anjanadurani@yahoo.co.in

Journal of Genetics and Genomics = Yi Chuan Xue Bao
|February 24, 2009
PubMed
Summary
This summary is machine-generated.

Histone tails, crucial for chromatin structure and gene regulation, undergo dynamic modifications. These modifications form a "histone code" that, when dysregulated, contributes to diseases like cancer.

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Last Updated: Jun 25, 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

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

Published on: May 5, 2022

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry
10:54

Extraction of Histones from Clinical Specimens for Epigenetic Profiling by Mass Spectrometry

Published on: November 21, 2025

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Biochemistry

Background:

  • The nucleosome, composed of DNA and histone proteins, is the fundamental unit of chromatin.
  • Histone N-terminal tails are dynamic regions extending from the nucleosome surface.
  • These tails are critical for higher-order chromatin structure and eukaryotic gene regulation.

Purpose of the Study:

  • To review complex histone tail modification patterns and their biological functions.
  • To explore the concept of the "histone code" in regulating chromatin structure and function.
  • To discuss the implications of histone modifications in human diseases, particularly cancer.

Main Methods:

  • Review of existing literature on histone modifications and chromatin biology.
  • Analysis of the role of post-translational modifications (e.g., methylation, acetylation, phosphorylation) on histone tails.
  • Examination of the "histone code" hypothesis and its implications.

Main Results:

  • Histone tails are extensively modified by various small chemical groups.
  • These modifications contribute to a combinatorial "histone code" interpreted by cellular machinery.
  • Dysregulation of this code is linked to human diseases, offering therapeutic potential.

Conclusions:

  • Histone tail modifications are central to epigenetic regulation of gene expression.
  • The "histone code" provides a complex regulatory layer influencing chromatin dynamics.
  • Understanding histone modification interplay is crucial for deciphering disease mechanisms and developing therapies.