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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,...
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...
Duplication of Chromatin Structure02:05

Duplication of Chromatin Structure

The process of chromosome duplication during cell division requires genome-wide disruption and re-assembly of chromatin. The chromatin structure must be accurately inherited, reassembled, and maintained in the daughter cells to ensure lineage propagation.
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...
The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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...
The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

SUMO: a multifaceted modifier of chromatin structure and function.

Caelin Cubeñas-Potts1, Michael J Matunis

  • 1Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.

Developmental Cell
|January 19, 2013
PubMed
Summary
This summary is machine-generated.

Small ubiquitin-related modifiers (SUMOs) are key regulators of chromatin structure and dynamics. SUMOylation influences gene expression and maintains genome integrity by modifying chromatin-associated proteins.

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Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
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Last Updated: May 15, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

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Published on: January 29, 2018

The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
24:02

The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin

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Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
06:23

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

Published on: April 27, 2019

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Genomics

Background:

  • Nuclear organization requires dynamic chromatin structures.
  • Posttranslational protein modifications regulate chromatin dynamics.
  • Small ubiquitin-related modifiers (SUMOs) are crucial regulators.

Purpose of the Study:

  • To review the role of SUMOylation in chromatin structure and function.
  • To summarize mechanisms by which SUMOylation impacts gene expression and genome integrity.

Main Methods:

  • Literature review of studies on SUMOylation and chromatin.
  • Analysis of research on posttranslational modifications of histones and chromatin factors.

Main Results:

  • SUMOylation regulates chromatin structure and function at multiple levels.
  • SUMOylation influences gene expression through diverse mechanisms.
  • SUMOylation plays a role in maintaining genome integrity.

Conclusions:

  • Posttranslational modification by SUMOs is essential for regulating chromatin.
  • SUMOylation is a critical mechanism for controlling gene expression and genome stability.