Related Experiment Video
Updated: Aug 3, 2025
08:16
In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
Published on: December 29, 2021
2.8K
Histone chaperones: A multinodal highway network inside the cell.
1Institute for Cancer Genetics, Columbia University Irving Medical Center, New York, NY 10032, USA; Herbert Irving Comprehensive Cancer Center, Columbia University Irving Medical Center, New York, NY 10032, USA; Department of Pediatrics, Columbia University Irving Medical Center, New York, NY 10032, USA; Department of Genetics and Development, Columbia University Irving Medical Center, New York, NY 10032, USA.
Molecular Cell
|April 7, 2023
Summary
Histone chaperones are key to DNA processes. A new study reveals an interconnected network and the surprising role of DAXX in depositing H3.3K9me3, impacting epigenetic inheritance.
Area of Science:
- Epigenetics and Molecular Biology
- Chromatin Biology
- Gene Regulation
Background:
- Histone chaperones are essential for managing histone proteins, crucial for DNA packaging into nucleosomes.
- These chaperones play vital roles in DNA replication, transcription, and epigenetic inheritance.
- Understanding histone chaperone networks is key to deciphering chromatin dynamics.
Purpose of the Study:
- To investigate the intricate network of histone chaperones.
- To uncover novel functions of histone chaperones in chromatin assembly.
- To elucidate the specific role of DAXX in the de novo deposition of H3.3K9me3.
Main Methods:
- Bioinformatic analysis of chaperone interactions.
- Biochemical assays to study histone deposition.
- Chromatin immunoprecipitation to assess H3.3K9me3 levels.
Main Results:
- Identification of a highly interconnected histone chaperone network.
- Demonstration of a previously unrecognized function for the histone chaperone DAXX.
- Evidence for DAXX-mediated de novo deposition of H3.3K9me3.
Conclusions:
- Histone chaperones form a complex, interconnected network critical for chromatin regulation.
- DAXX plays a surprising and direct role in the deposition of the repressive histone mark H3.3K9me3.
- These findings advance our understanding of epigenetic mechanisms and histone dynamics.
Related Concept Videos
02:30Histone Variants at the Centromere
4.4K
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...
4.4K
02:54Nucleosome Remodeling
9.2K
Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
9.2K
02:21Chromatin Packaging
15.6K
Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter?
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...
15.6K
02:32Histone Modification
13.4K
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...
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone...
13.4K
01:32Cytoskeletal Coordination in Cell Migration
4.8K
A migrating cell changes its shape during the cyclic events of attachment and detachment from the substratum and repositions the cell organelles correspondingly. These complex events are orchestrated by the dynamic cytoskeletal network comprising actin filaments, intermediate filaments, and microtubules. Cytoskeletal crosstalk — the direct and indirect communication between the different components — is crucial for this coordination. Direct communication involves various linker...
4.8K
02:33The Nucleosome
16.4K
DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
DNA is wound twice around a protein complex called histone core, that consist of 8 histone proteins. This complex...
16.4K