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Related Concept Videos

Histone Modification02:32

Histone Modification

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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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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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Heterochromatin02:38

Heterochromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions that take up more dye are called heterochromatin. Heterochromatin is further classified into two forms – constitutive heterochromatin and facultative heterochromatin.
Constitutive heterochromatin: It is a highly compact region of chromatin that is mostly concentrated in the centromere and telomere. Unlike euchromatin, the amino acid at...
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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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Euchromatin01:01

Euchromatin

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The extent of chromatin compaction can be studied by staining chromatin using specific DNA binding dyes. Under the microscope, the dense-compacted regions take up more dye, appearing darker, while the less-compact areas take up less dye and appear lighter. Based on the compaction level, chromatins are classified into two primary forms – euchromatin and heterochromatin.
Euchromatin is the less dense region of the chromatin and stains lighter. Euchromatin contains histone H3 extensively...
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Chromatin Packaging02:21

Chromatin Packaging

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Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...
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Modus operandi: Chromatin recognition by α-helical histone readers.

Hossein Davarinejad1, Alexis Arvanitis-Vigneault1, Dallas Nygard1

  • 1Ottawa Institute of Systems Biology, Department of Biochemistry, Microbiology and Immunology, Faculty of Medicine, University of Ottawa, 451 Smyth Road, Ottawa, ON K1H 8M5, Canada.

Structure (London, England : 1993)
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Summary

Histone reader domains recognize histone post-translational modifications (PTMs) using diverse α-helical folds. This review compares how these protein domains achieve varied structures and peptide-binding mechanisms for distinct target recognition.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Histone reader domains are crucial for interpreting the nuclear environment.
  • These domains recognize histone post-translational modifications (PTMs), regulating gene expression and nuclear processes.
  • Several families of histone readers exist, including 14-3-3s, ankyrin repeat domains (ARDs), tetratricopeptide repeats (TPRs), bromodomains (BRDs), and HEAT domains.

Purpose of the Study:

  • To review and compare the structural diversity and peptide-binding mechanisms of various histone reader domains.
  • To highlight how different folding strategies lead to distinct recognition of histone modifications.
  • To provide insights into the functional implications of diverse histone reader structures.

Main Methods:

  • Comparative analysis of structural data for different histone reader domains.
  • Review of literature on histone reader-PTM interactions.
  • Examination of the α-helical fold commonality and tertiary structure variations.

Main Results:

  • Histone reader domains, despite sharing an α-helical fold, exhibit significant diversity in their tertiary structures.
  • These structural variations enable distinct peptide-binding mechanisms.
  • The binding footprints of targets are vastly different across these reader domains.

Conclusions:

  • The structural plasticity of histone reader domains allows for specialized recognition of histone marks.
  • Understanding these diverse structures is key to deciphering the complex epigenetic landscape.
  • This comparative review offers a framework for future research into histone code interpretation.