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Related Concept Videos

Histone Modification02:32

Histone Modification

14.9K
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...
14.9K
Histone Modification02:32

Histone Modification

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Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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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...
8.9K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.7K
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...
4.7K
Inheritance of Chromatin Structures03:17

Inheritance of Chromatin Structures

6.9K
Epigenetics is the study of inherited changes in a cell's phenotype without changing the DNA sequences. It provides a form of memory for the differential gene expression pattern to maintain cell lineage, position-effect variegation, dosage compensation, and maintenance of chromatin structures such as telomeres and centromeres. For example, the structure and location of the centromere on chromosomes are epigenetically inherited. Its functionality is not dictated or ensured by the underlying...
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Related Experiment Video

Updated: Nov 10, 2025

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue

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Combinatorial Histone H3 Modifications Are Dynamically Altered in Distinct Cell Cycle Phases.

Congcong Lu1, Mariel Coradin1,2, Kevin A Janssen1,2

  • 1Epigenetics Institute, Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.

Journal of the American Society for Mass Spectrometry
|April 5, 2021
PubMed
Summary

Histone post-translational modifications (PTMs) are crucial for cell cycle regulation and cancer. This study reveals cell cycle-dependent histone PTMs, highlighting their role in proliferation and potential as cancer biomarkers.

Keywords:
H3 variantscell cyclehistone modificationsmiddle-downquantitative proteomics

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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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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Related Experiment Videos

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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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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Proteomics

Background:

  • Histones are key to chromatin structure, and their post-translational modifications (PTMs) regulate DNA access and chromosome condensation.
  • Dysregulation of cell cycle and histone PTMs is linked to diseases like cancer.
  • Understanding histone PTMs offers insights into epigenetic regulation of cell proliferation.

Purpose of the Study:

  • To apply a novel middle-down workflow for high-throughput analysis of histone PTMs during the cell cycle.
  • To investigate histone H3.1 and H3.2 modifications throughout the cell cycle.
  • To identify cell cycle-dependent and variant-specific histone modifications.

Main Methods:

  • Utilized a novel middle-down proteomics workflow with porous graphitic carbon (PGC) stationary phase.
  • Employed reversed-phase chromatography coupled with online mass spectrometry (MS).
  • Analyzed histone H3.1 and H3.2 modifications during different cell cycle phases.

Main Results:

  • Identified 1133 uniquely modified canonical histone H3 N-terminal tails.
  • Observed increased histone H3 phosphorylation during mitosis (M phase).
  • Confirmed cell cycle-dependent and variant-specific PTMs for H3.1 and H3.2, revealing PTM crosstalk.

Conclusions:

  • Combinatorial histone PTMs are implicated in cell cycle control.
  • Histone H3.1 and H3.2 modifications are distinct and should not be analyzed together.
  • Identified histone PTMs may serve as proliferation markers for cancer research.