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Related Concept Videos

Histone Modification02:32

Histone Modification

14.5K
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...
14.5K
Histone Modification02:32

Histone Modification

4.0K
4.0K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.1K
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...
8.1K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

2.6K
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...
2.6K
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

12.1K
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...
12.1K
Histone Variants at the Centromere02:30

Histone Variants at the Centromere

4.0K
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...
4.0K

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Assays for Validating Histone Acetyltransferase Inhibitors
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Histone mimics: digging down under.

Yiwei Lin1, Binhua P Zhou1

  • 1Departments of Molecular and Cellular Biochemistry, and Markey Cancer Center, College of Medicine, The University of Kentucky, Lexington, KY 40506, USA.

Frontiers in Biology
|June 27, 2014
PubMed
Summary
This summary is machine-generated.

Epigenetic deregulation drives human diseases. This review explores a novel histone mimicry strategy used by enzymes to target non-histone proteins, offering potential diagnostic and therapeutic insights.

Keywords:
epigeneticshistone mimicry

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Area of Science:

  • Biochemistry and Molecular Biology
  • Epigenetics
  • Disease Mechanisms

Background:

  • Epigenetic deregulation is a key factor in human disease development.
  • Histone-modifying enzymes are known to target non-histone proteins, but the mechanism is unclear.
  • Understanding these mechanisms is crucial for advancing diagnostics and therapeutics.

Purpose of the Study:

  • To review the novel histone mimicry strategy in non-histone substrate recognition.
  • To discuss the potential clinical implications of this epigenetic mechanism.
  • To provide insights into enzyme activity beyond histone modification.

Main Methods:

  • Literature review focusing on histone mimicry.
  • Analysis of enzyme substrate recognition mechanisms.
  • Discussion of clinical relevance and future research directions.

Main Results:

  • Identification of histone mimicry as a widespread strategy for non-histone protein targeting by enzymes.
  • Elucidation of how enzymes recognize and modify non-histone substrates.
  • Highlighting the significance of this mechanism in disease pathology.

Conclusions:

  • Histone mimicry is a critical, yet underappreciated, mechanism in epigenetic regulation.
  • Targeting this pathway offers promising avenues for novel disease diagnostics and therapies.
  • Further research is warranted to fully exploit the clinical potential of histone mimicry.