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Related Concept Videos

Histone Modification02:32

Histone Modification

15.5K
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

Histone Modification

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Hypoxia01:23

Hypoxia

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Hypoxia is a medical condition characterized by an inadequate oxygen supply to body tissues. It typically manifests as a bluish discoloration of the skin and mucosae, especially in fair-skinned individuals, when hemoglobin (Hb) saturation drops below 75%.
Types of Hypoxia
There are four primary types of hypoxia, each resulting from a different cause:
1. Anemic hypoxia: This type occurs due to insufficient oxygen delivery caused by a lack of red blood cells (RBCs) or RBCs with abnormal or...
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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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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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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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Related Experiment Video

Updated: Dec 16, 2025

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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Hypoxia and hypoxia mimetics differentially modulate histone post-translational modifications.

Kuo-Feng Hsu1,2, Sarah E Wilkins1, Richard J Hopkinson1,3

  • 1Chemistry Research Laboratory, Department of Chemistry, University of Oxford , Oxford, UK.

Epigenetics
|July 2, 2020
PubMed
Summary

Synthetic hypoxia mimetics do not fully replicate physiological hypoxia's effects on histone post-translational modifications (PTMs). Intact protein LC-MS profiling reveals distinct PTM changes, cautioning against direct comparisons.

Keywords:
2-oxoglutarate/α-ketoglutarate oxygenasesHIFHypoxiaepigeneticshistone post-translational modificationshypoxia mimeticsintact protein mass spectrometryiron chelating drugs

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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:

  • Biochemistry
  • Epigenetics
  • Molecular Biology

Background:

  • Post-translational modifications (PTMs) on histone tails are crucial for epigenetic regulation.
  • Hypoxia influences histone modifications via histone-modifying enzymes and hypoxia-inducible factors (HIFs).

Purpose of the Study:

  • To investigate the accuracy of synthetic hypoxia mimetics in replicating hypoxia's effects on histone PTMs.
  • To profile global changes in histone PTMs under hypoxia and hypoxia-mimicking conditions.

Main Methods:

  • Utilized liquid chromatography-mass spectrometry (LC-MS) for intact protein profiling.
  • Analyzed global changes in PTMs on core histone proteins.

Main Results:

  • Intact protein LC-MS profiling is a robust method for assessing drug effects on histone modifications.
  • Identified distinct PTM profiles between physiological hypoxia and chemically induced hypoxia.
  • Demonstrated that hypoxia mimetics do not completely mimic the PTM changes induced by physiological hypoxia.

Conclusions:

  • Chemically induced hypoxia using mimetics does not fully replicate the impact of physiological hypoxia on histone PTMs.
  • Caution is advised when interpreting data from hypoxia mimetics due to incomplete mimicry of hypoxic effects on histones.