Jove
Visualize
Contact Us

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,...
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...
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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Discovery and biological evaluation of HS13 as a novel covalent ligand targeting the NSD2-PWWP1 domain.

Bioorganic & medicinal chemistry·2026
Same author

ChatMDV: Reducing Technical Barriers in Bioinformatics Analysis using Large Language Models.

GigaScience·2026
Same author

Identification of novel covalent ligands that disrupt Acetyl-Lysine binding to the SETDB1 tudor domain.

Biochemical and biophysical research communications·2026
Same author

Structure-based design of the approved drug zafirlukast identifies HLC40 as a potent WDR5 WIN-site inhibitor with antitumor efficacy.

Bioorganic chemistry·2026
Same author

Development of a Dual Chemical Probe for the USP16 and HDAC6 Zinc-Finger Ubiquitin-Binding Domain.

Journal of medicinal chemistry·2026
Same author

Structural basis for sequence-specific DNA recognition by a group IId WRKY transcription factor GhWRKY17 in cotton.

The Biochemical journal·2026
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Video

Updated: Jun 9, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Structural genomics of histone tail recognition.

Minghua Wang1, Man Wai Mok, Hong Harper

  • 1Structural Genomics Consortium, University of Oxford, Headington, Oxford OX37DQ, UK.

Bioinformatics (Oxford, England)
|August 27, 2010
PubMed
Summary

This web server provides interactive 3D structures of histone tail recognition by human proteins. It aids in understanding epigenetic signaling and designing new inhibitors.

More Related Videos

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

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

Related Experiment Videos

Last Updated: Jun 9, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
06:32

Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

Published on: March 9, 2022

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

Area of Science:

  • Structural biology
  • Epigenetics
  • Computational biology

Background:

  • Histone tails are crucial epigenetic modifiers.
  • Understanding their interactions with proteins is key to epigenetic regulation.
  • Publicly available structural data is fragmented.

Purpose of the Study:

  • To create a centralized, accessible resource for histone tail recognition structures.
  • To facilitate the analysis of structural mechanisms in epigenetic signaling.
  • To support drug discovery efforts targeting epigenetic pathways.

Main Methods:

  • Compilation of publicly available experimental structures.
  • Development of an interactive web server with 3D visualizations.
  • Integration of concise textual explanations linked to graphics.

Main Results:

  • A comprehensive web server detailing histone tail-protein complexes.
  • Interactive 3D modules illustrating recognition mechanisms.
  • Analysis of binding modes and chemical tractability.

Conclusions:

  • The resource enables comparative analysis of histone recognition.
  • It aids in evaluating druggability of epigenetic targets.
  • Facilitates the design of small molecule inhibitors for epigenetic modulation.