Jove
Visualize
Contact Us
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 Concept Videos

Histone Modification02:32

Histone Modification

16.2K
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...
16.2K
Histone Modification02:32

Histone Modification

4.5K
4.5K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

5.1K
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...
5.1K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

19.8K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
19.8K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.0K
15.0K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

14.5K
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...
14.5K

You might also read

Related Articles

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

Sort by
Same author

Soluble N-Terminal Domain of the Prion Protein Interferes with Fibrillization of α-Synuclein to Form Off-Pathway Assemblies that Lack Cellular Seeding Activity.

ACS chemical neuroscience·2025
Same author

Defective IFT57 underlies a novel cause of Bardet-Biedl syndrome.

Human molecular genetics·2025
Same author

Topological confinement by a membrane anchor suppresses phase separation into protein aggregates: Implications for prion diseases.

Proceedings of the National Academy of Sciences of the United States of America·2024
Same author

Replisome Proximal Protein Associations and Dynamic Proteomic Changes at Stalled Replication Forks.

Molecular & cellular proteomics : MCP·2024
Same author

NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62.

Nature communications·2023
Same author

Antagonistic roles of canonical and Alternative-RPA in disease-associated tandem CAG repeat instability.

Cell·2023
Same journal

Genomic Imprinting: Common Threads Uniting Diverse Biological Systems.

Annual review of genetics·2026
Same journal

Properties and Prospects of B Chromosomes.

Annual review of genetics·2026
Same journal

Lessons From Yeast: Mechanisms of Telomere Length Regulation.

Annual review of genetics·2026
Same journal

Mechanisms and Evolutionary Advantages of Unlimited Reproductive Lifespans in Naked Mole-Rat Queens.

Annual review of genetics·2026
Same journal

Impact of Small RNA Sponges on Regulatory RNA Networks in Bacteria.

Annual review of genetics·2025
Same journal

Context Specificity of MAP3K DLK Signaling in the Nervous System: Insights from Genetics and Genomics.

Annual review of genetics·2025
See all related articles

Related Experiment Video

Updated: Feb 5, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

22.2K

H3-H4 Histone Chaperone Pathways.

Prerna Grover1, Jonathon S Asa2, Eric I Campos1,2

  • 1Genetics & Genome Biology Program, The Hospital for Sick Children, Toronto, Ontario M5G 0A4, Canada;

Annual Review of Genetics
|September 6, 2018
PubMed
Summary
This summary is machine-generated.

Histone chaperones are crucial for managing nucleosome structure and chromatin accessibility. This review details canonical and variant H3-H4 histone chaperone pathways involved in depositing histones onto DNA.

Keywords:
chromatinhistonehistone chaperonenucleosome

More Related Videos

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

3.2K
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

2.2K

Related Experiment Videos

Last Updated: Feb 5, 2026

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue
09:43

Purification of H3 and H4 Histone Proteins and the Quantification of Acetylated Histone Marks in Cells and Brain Tissue

Published on: November 30, 2018

22.2K
In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

3.2K
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

2.2K

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chromatin Biology

Background:

  • Nucleosomes, fundamental units of DNA packaging, regulate genetic material accessibility.
  • Chromatin accessibility is dynamically modulated by nucleosome positioning, histone variants, and posttranslational modifications.
  • Histone chaperones are essential for the dynamic processing, deposition, and eviction of histones.

Purpose of the Study:

  • To review the molecular mechanisms of canonical and variant H3-H4 histone chaperone pathways.
  • To elucidate the processes of histone deposition onto DNA.
  • To highlight the roles of specialized chaperones in histone variant deposition.

Main Methods:

  • Review of established literature on histone chaperone pathways.
  • Focus on molecular details of H3-H4 histone deposition.
  • Discussion of replication-coupled and replication-independent pathways.

Main Results:

  • Detailed understanding of H3-H4 histone folding, posttranslational modification, and nuclear import.
  • Elucidation of replication-coupled H3.1-H4 deposition during S-phase.
  • Explanation of replication-independent H3.3-H4 deposition via alternative pathways.

Conclusions:

  • Histone chaperone pathways are critical for maintaining chromatin dynamics and gene regulation.
  • Distinct pathways govern the deposition of canonical and variant histones.
  • Specialized chaperones ensure precise deposition of histone variants for specific cellular functions.