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Related Concept Videos

Histone Modification02:32

Histone Modification

14.6K
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...
14.6K
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

7.8K
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....
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Proteomics01:33

Proteomics

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A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
8.4K
Protein Networks02:26

Protein Networks

4.1K
An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.1K
Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

8.7K
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...
8.7K
Protein-protein Interfaces02:04

Protein-protein Interfaces

14.0K
Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
14.0K

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Related Experiment Video

Updated: Oct 11, 2025

Global Level Quantification of Histone Post-Translational Modifications in a 3D Cell Culture Model of Hepatic Tissue
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Mapping histone modification-dependent protein interactions with chemical proteomics.

Yanmei Chen1, Yi Wang2

  • 1State Key Laboratory of Plant Physiology and Biochemistry, College of Biological Sciences, China Agricultural University, 100193, Beijing, China.

Trends in Biochemical Sciences
|December 7, 2021
PubMed
Summary

Histone post-translational modifications (PTMs) are key to epigenetics. Chemical proteomics offers a way to map the proteins that interact with these crucial histone PTMs for better understanding of gene regulation.

Keywords:
crosslinkdiseaseepigeneticphosphorylationprotein–protein interactionsproximity biotinylation

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The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
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Last Updated: Oct 11, 2025

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Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
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The ChroP Approach Combines ChIP and Mass Spectrometry to Dissect Locus-specific Proteomic Landscapes of Chromatin
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Chemical Biology

Background:

  • Histone post-translational modifications (PTMs) are critical regulators of chromatin structure and function.
  • These modifications influence gene expression and are implicated in various developmental and pathological processes.
  • Understanding the proteins that interact with histone PTMs is essential for deciphering epigenetic regulatory mechanisms.

Purpose of the Study:

  • To highlight the application of chemical proteomics for studying histone PTMs.
  • To emphasize the potential for simultaneous and global exploration of histone PTM interaction networks.

Main Methods:

  • Utilizing chemical proteomics techniques.
  • Focusing on the simultaneous and global analysis of protein interactions.

Main Results:

  • Demonstrates the feasibility of using chemical proteomics to identify interaction partners of histone PTMs.
  • Provides a framework for comprehensive mapping of epigenetic regulatory networks.

Conclusions:

  • Chemical proteomics is a powerful approach for dissecting the functional landscape of histone PTMs.
  • This methodology enables a deeper understanding of the interplay between histone modifications and transcriptional regulation.