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Related Concept Videos

Histone Modification02:32

Histone Modification

16.0K
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...
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Histone Modification02:32

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Spreading of Chromatin Modifications02:25

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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...
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Chromatin Structure Regulates pre-mRNA Processing02:41

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In eukaryotic cells, nascent mRNA transcripts need to undergo many post-transcriptional modifications to reach the cell cytoplasm and translate into functional proteins. For a long time, transcription and pre-mRNA processing were considered two independent events that occur sequentially in the cell. However, it has now been well established that transcription and pre-mRNA processing are two simultaneous processes that are precisely regulated inside the cell.
The chromatin structure, especially...
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Histone Variants at the Centromere02:30

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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...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
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Updated: Jan 22, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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ATAD2 mediates chromatin-bound histone chaperone turnover.

Ariadni Liakopoulou1, Fayçal Boussouar1, Daniel Perazza1

  • 1Université Grenoble Alpes, INSERM U1209, CNRS UMR 5309, Institute for Advanced Biosciences, Grenoble, France.

Elife
|January 20, 2026
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Summary

The protein ATAD2 regulates chromatin plasticity and histone chaperone turnover. This study shows ATAD2 is crucial for genome organization and gene transcription during mouse spermatogenesis.

Keywords:
Atad2Spermatogenesischaperone turnoverchromatin dynamicschromosomesgene expressionmouse

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Area of Science:

  • Molecular Biology
  • Genetics
  • Cell Biology

Background:

  • ATAD2 (ATPase Associated With Diverse Budgets 2) is a conserved protein found in embryonic stem (ES) cells and spermatogenic cells.
  • Previous studies highlighted ATAD2's role in chromatin-bound histone chaperone turnover in ES cells and S. pombe.

Purpose of the Study:

  • To investigate the function of ATAD2 in mouse spermatogenesis.
  • To elucidate ATAD2's role in chromatin condensation and genome packaging in mature sperm.

Main Methods:

  • Focusing on mouse spermatogenesis.
  • Investigating ATAD2's regulation of HIRA-dependent H3.3 localization and transcription.
  • Analyzing the impact of Atad2 disruption on genome organization.

Main Results:

  • ATAD2 regulates H3.3 localization and transcription during mouse spermatogenesis.
  • ATAD2 modulates histone eviction and protamine assembly for chromatin condensation.
  • Disruption of Atad2 leads to abnormal genome organization in mature spermatozoa.

Conclusions:

  • ATAD2 governs a critical level of chromatin dynamic regulation via histone chaperone binding.
  • ATAD2 controls the balance between histone deposition and removal, essential for proper genome packaging.