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Related Concept Videos

Histone Modification02:32

Histone Modification

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 deacetylase,...
Histone Modification02:32

Histone Modification

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 deacetylase,...
Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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...
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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 is an enzyme that can...

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Updated: Jul 3, 2026

Detection of Histone Modifications in Plant Leaves
07:08

Detection of Histone Modifications in Plant Leaves

Published on: September 23, 2011

Formaldehyde-induced histone modifications in vitro.

Kun Lu1, Gunnar Boysen, Lina Gao

  • 1Curriculum in Applied Science & Engineering, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.

Chemical Research in Toxicology
|July 29, 2008
PubMed
Summary
This summary is machine-generated.

Formaldehyde causes DNA-protein cross-links by binding to histone lysine. This binding, which is blocked by post-translational modifications, may disrupt epigenetic regulation.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Toxicology

Background:

  • Formaldehyde is a known genotoxic and mutagenic agent.
  • Formaldehyde induces DNA-protein cross-links (DPC), with histones implicated in their formation.
  • The reaction mechanism involves lysine epsilon-amino groups and DNA exocyclic amino groups.

Purpose of the Study:

  • To identify specific binding sites of formaldehyde on histones.
  • To investigate the role of post-translational modifications (PTM) in formaldehyde-histone interactions.
  • To explore the potential impact of formaldehyde on epigenetic regulation.

Main Methods:

  • Mass spectrometry was employed to identify histone binding sites for formaldehyde.
  • Analysis focused on lysine residues in histone N-terminal tails and globular domains.
  • Investigated the influence of PTM on formaldehyde binding and Schiff base formation.

Main Results:

  • Formaldehyde binds to the N-terminus of histone and lysine residues in both N-terminal tails and globular domains.
  • Only unmodified lysine residues are susceptible to formaldehyde attack, indicating PTM blocks binding.
  • Formaldehyde-induced Schiff bases on lysine inhibit PTM formation, suggesting interference with epigenetic regulation.

Conclusions:

  • Formaldehyde directly interacts with histones at specific lysine residues.
  • Post-translational modifications on histones prevent formaldehyde binding.
  • Formaldehyde may alter epigenetic regulation by inhibiting histone PTM formation.