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Related Concept Videos

Histone Modification02:32

Histone Modification

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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

Spreading of Chromatin Modifications

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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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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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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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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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...
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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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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...
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Related Experiment Video

Updated: Dec 11, 2025

Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
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Histone H1 Post-Translational Modifications: Update and Future Perspectives.

Marta Andrés1, Daniel García-Gomis1,2, Inma Ponte1

  • 1Biochemistry and Molecular Biology Department, Biosciences Faculty, Autonomous University of Barcelona, 08193 Cerdanyola del Vallès, Spain.

International Journal of Molecular Sciences
|August 23, 2020
PubMed
Summary
This summary is machine-generated.

Histone H1, a highly variable protein, has numerous post-translational modifications (PTMs) influencing chromatin structure, cell cycle, and disease. This review details H1 PTMs and their functions across species.

Keywords:
PTM functionacetylationchromatin structurecitrullinationdiseasehistone H1mass spectrometrymethylationphosphorylationubiquitylation

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Proteomics

Background:

  • Histone H1 is a key regulator of chromatin structure, distinct from core histones.
  • H1 exhibits significant variability, with multiple subtypes and extensive post-translational modifications (PTMs).
  • The functional roles of H1 PTMs are less understood compared to core histone modifications.

Purpose of the Study:

  • To review and summarize known histone H1 post-translational modifications (PTMs) across eukaryotes, with a focus on mammals.
  • To highlight PTMs with characterized molecular functions.
  • To examine the association of H1 PTMs with biological processes and diseases.

Main Methods:

  • Literature review and synthesis of existing research on histone H1 PTMs.
  • Focus on mass spectrometry-based proteomics data.
  • Analysis of studies describing the functional and disease-related roles of H1 PTMs.

Main Results:

  • Histone H1 undergoes a wide array of PTMs, with increasing complexity identified through proteomics.
  • PTMs in H1 are linked to chromatin organization, cell cycle progression, gene transcription, DNA repair, and differentiation.
  • Specific H1 PTMs are implicated in diseases including cancer, autoimmune disorders, and viral infections.

Conclusions:

  • Histone H1 PTMs play crucial roles in diverse cellular functions and are implicated in various pathologies.
  • Further research is needed to fully elucidate the functional significance and regulatory mechanisms of H1 PTMs.
  • Advanced profiling techniques are essential for comprehensive understanding of the H1 PTM landscape.