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Related Concept Videos

Histone Modification02:32

Histone Modification

13.7K
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...
13.7K
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...
8.5K
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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.0K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
7.0K
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

1.1K
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.
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...
1.1K
Heterochromatin02:38

Heterochromatin

14.2K
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...
14.2K

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Related Experiment Video

Updated: Aug 28, 2025

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

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Decoding histone ubiquitylation.

Jennifer J Chen1, Dylan Stermer1, Jason C Tanny1

  • 1Department of Pharmacology and Therapeutics, McGill University, Montreal, QC, Canada.

Frontiers in Cell and Developmental Biology
|September 15, 2022
PubMed
Summary
This summary is machine-generated.

Histone ubiquitylation, a key epigenetic mark, regulates gene expression and DNA repair. This review explores how "reader" proteins recognize these marks, influencing cellular processes and disease.

Keywords:
53BP1BARD1 BRCTDOT1lDnmt1PRC1 and PRC2 recruitmenthistone modification readershistone ubiquitylationubiquitin signaling

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Area of Science:

  • Epigenetics and Molecular Biology
  • Gene Regulation
  • DNA Damage Response

Background:

  • Histone ubiquitylation is crucial for active and repressed transcription, and DNA damage signaling.
  • Enzymes modifying histones are vital for cell growth, development, and disease across species.
  • The molecular consequences of histone ubiquitylation are increasingly understood.

Purpose of the Study:

  • To review the structure and function of proteins that read histone ubiquitylation marks.
  • To highlight how ubiquitin recognition provides specificity and function to molecular interactions.
  • To discuss implications for understanding histone modifications broadly.

Main Methods:

  • Literature review of structural and functional studies.
  • Analysis of protein-effector interactions.
  • Synthesis of current knowledge on histone ubiquitylation readers.

Main Results:

  • Histone ubiquitylation readers are key mediators of downstream signaling.
  • Ubiquitin recognition by readers confers specificity in transcription and DNA repair.
  • These interactions are fundamental to cellular processes.

Conclusions:

  • Understanding histone ubiquitylation readers is essential for deciphering epigenetic regulation.
  • Reader proteins provide a critical link between histone marks and cellular outcomes.
  • This knowledge advances our broader comprehension of histone modifications and their roles in health and disease.