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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,...
Cytotoxic T Cells-mediated Immune Response01:27

Cytotoxic T Cells-mediated Immune Response

Cytotoxic T cells are a vital component of the immune system. They have the remarkable ability to identify and target antigens on infected or abnormal cells. These antigens often originate from intracellular pathogens such as viruses or abnormal proteins cancer cells produce.
Immunological surveillance is the ability of immune cells to monitor and eliminate infected cells with intracellular pathogens, neoplastically transformed cells, and cells with non-self antigens. Cytotoxic T cells and NK...
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...
Hypersensitivity Reactions: Cytolytic Reactions01:01

Hypersensitivity Reactions: Cytolytic Reactions

Type II hypersensitivity involves IgG and IgM antibodies targeting cell surface antigens, leading to cell destruction. This can occur through complement activation, antibody-dependent cell-mediated cytotoxicity (ADCC), or acting as opsonins for phagocytosis. When excessive, these reactions cause significant tissue damage.Drug-induced hemolytic anemia is a common example, where drugs like penicillin or cephalosporins bind to red blood cells, forming drug-protein complexes. These complexes...
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 8, 2026

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

Excess histone levels mediate cytotoxicity via multiple mechanisms.

Rakesh Kumar Singh1, Dun Liang, Ugander Reddy Gajjalaiahvari

  • 1Department of Biomedical Sciences, College of Medicine, Florida State University, Tallahassee, Florida, USA.

Cell Cycle (Georgetown, Tex.)
|October 16, 2010
PubMed
Summary

Excess histones cause genomic instability and cell death by interfering with DNA/RNA metabolism and enzyme activity. This occurs through inappropriate electrostatic interactions, highlighting the need for tight histone regulation.

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Related Experiment Videos

Last Updated: Jun 8, 2026

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

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

Unveiling Histone Proteoforms using 2D-TAU Gel Electrophoresis

Published on: October 18, 2024

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:

  • Cell Biology
  • Genetics
  • Molecular Biology

Background:

  • Histone protein accumulation leads to genomic instability, increased DNA damage sensitivity, and cytotoxicity.
  • Histone synthesis is tightly regulated transcriptionally and posttranscriptionally.
  • Recent findings show posttranslational regulation by Rad53 and proteasome-dependent proteolysis in yeast.

Purpose of the Study:

  • Investigate the mechanistic basis of deleterious effects from excess histones in budding yeast.
  • Elucidate how excess histones impact cellular processes and viability.

Main Methods:

  • Budding yeast model system.
  • Histone protein overexpression.
  • Microarray analysis to assess gene expression changes.
  • Investigated interactions with DNA, RNA, and modifying enzymes.

Main Results:

  • Excess histones saturate histone modifying enzymes, impairing their function.
  • Non-specific binding of excess histones to DNA and RNA disrupts their metabolism.
  • Microarray analysis revealed significant upregulation or downregulation of approximately 240 genes upon histone overexpression.
  • Cytotoxic effects are mediated by inappropriate electrostatic interactions.

Conclusions:

  • Excess histones exert deleterious effects through multiple mechanisms, primarily driven by electrostatic interactions.
  • Findings explain the necessity for stringent histone level control.
  • Maintaining proper histone levels is crucial for genomic stability and cell viability.