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Related Concept Videos

Histone Modification02:32

Histone Modification

14.6K
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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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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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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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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Human Coronavirus 229E Infection Alters Histone Proteoforms.

Ashley N Ives1, Stephanie Thibert1, Madelyn R Berger2

  • 1Environmental Molecular Sciences Division, Pacific Northwest National Laboratory, Richland, Washington 99354, United States.

Journal of Proteome Research
|April 28, 2026
PubMed
Summary
This summary is machine-generated.

Human coronavirus 229E infection alters histone proteoforms in lung cells. Top-down proteomics revealed decreased histone truncation, suggesting viruses modify histone length to control host gene expression.

Keywords:
HCoV-229 infectionhistoneproteoformstop–down proteomicstruncation

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Area of Science:

  • Virology
  • Proteomics
  • Epigenetics

Background:

  • Viruses utilize host epigenetic mechanisms, including histone modifications, to manipulate host gene expression for replication.
  • Understanding how viruses alter host epigenetics is crucial for deciphering viral pathogenesis.

Purpose of the Study:

  • To investigate changes in histone proteoforms in lung fibroblast cells upon human coronavirus 229E (HCoV-229E) infection.
  • To explore the role of histone truncation in viral-host interactions.

Main Methods:

  • Top-down proteomics was used to quantify histone proteoforms in HCoV-229E-infected and mock-infected MRC-5 cells.
  • Differential abundance analysis was performed to identify changes in histone proteoform levels and modifications.

Main Results:

  • A total of 572 proteoforms were identified, with 461 assigned to core histones (H2A, H2B, H3, H4).
  • 200 histone proteoforms were quantifiable, showing differential abundance in response to HCoV-229E infection.
  • A significant decrease in truncated histone proteoforms, specifically C-terminally truncated H2A and N-terminally truncated H3, was observed in infected cells.

Conclusions:

  • Top-down proteomics effectively resolves unique histone proteoform truncation states.
  • HCoV-229E infection alters histone proteoform abundance and truncation patterns.
  • These findings support the hypothesis that viruses modify histone length to influence host gene expression.