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Related Concept Videos

Epigenetic Regulation01:37

Epigenetic Regulation

Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...
Epigenetic Regulation01:46

Epigenetic Regulation

Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
Epigenetic Regulation01:46

Epigenetic Regulation

Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
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...

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Related Experiment Video

Updated: May 11, 2026

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
11:02

Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis

Published on: May 17, 2016

Readout of epigenetic modifications.

Dinshaw J Patel1, Zhanxin Wang

  • 1Structural Biology Department, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA. pateld@mskcc.org

Annual Review of Biochemistry
|May 7, 2013
PubMed
Summary
This summary is machine-generated.

This review explores how histone posttranslational modifications (PTMs) are read by protein modules, influencing gene regulation and disease. Understanding these interactions offers new therapeutic strategies for epigenetic diseases.

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Complete Workflow for Analysis of Histone Post-translational Modifications Using Bottom-up Mass Spectrometry: From Histone Extraction to Data Analysis
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Area of Science:

  • Epigenetics and Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Histone posttranslational modifications (PTMs) are crucial epigenetic marks that regulate chromatin structure and function.
  • Reader modules recognize these PTMs, recruiting effector proteins to modulate gene expression, DNA repair, and other cellular processes.
  • Dysregulation of histone PTM readout is implicated in various diseases, including cancer and developmental disorders.

Purpose of the Study:

  • To provide a structure-based analysis of how histone PTMs are recognized by reader proteins.
  • To elucidate the principles governing the recognition of diverse histone marks, including methylation, acetylation, and phosphorylation.
  • To discuss the implications of histone PTM readout in gene regulation, disease, and therapeutic interventions.

Main Methods:

  • Structure-based analysis of protein-PTM interactions.
  • Review of existing literature on histone PTM readers and their binding pockets.
  • Analysis of multivalent readout mechanisms and crosstalk between PTMs.

Main Results:

  • Detailed insights into the diverse architectures of reader-binding pockets for various histone PTMs.
  • Common principles underlying the specific recognition of methyl-lysine, methyl-arginine, acetyl-lysine, and phosphoserine marks.
  • The significant impact of multivalent PTM readout on biological processes like transcription and repair.

Conclusions:

  • Structural understanding of histone PTM readout is essential for deciphering epigenetic regulation.
  • Targeting histone PTM reader interactions presents promising therapeutic avenues for epigenetic diseases.
  • Future research should focus on nucleosome-level mechanistic and structural insights into histone PTM readout.