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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...
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...
Heterochromatin02:38

Heterochromatin

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 9th...

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Related Experiment Video

Updated: Jun 25, 2026

Analysis of Histone Antibody Specificity with Peptide Microarrays
09:47

Analysis of Histone Antibody Specificity with Peptide Microarrays

Published on: August 1, 2017

Structure and function of histone methylation binding proteins.

Melanie A Adams-Cioaba1, Jinrong Min

  • 1Structural Genomics Consortium, University of Toronto, Toronto, ONM5G1L6, Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|February 24, 2009
PubMed
Summary
This summary is machine-generated.

Histone modifications regulate chromatin function, with histone methylation being key. This review details how PHD, Tudor, and MBT domains recognize histone peptides, clarifying complex mechanisms.

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Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
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Analysis of Histone Antibody Specificity with Peptide Microarrays
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Isolation and Cultivation of Neural Progenitors Followed by Chromatin-Immunoprecipitation of Histone 3 Lysine 79 Dimethylation Mark
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Chromatin Immunoprecipitation (ChIP) of Histone Modifications from Saccharomyces cerevisiae
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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Structural Biology

Background:

  • Chromatin structure is dynamically regulated by various factors, including histone modifications.
  • Histone modifications, particularly methylation, play crucial roles in fundamental cellular processes like DNA replication, repair, and transcription.
  • The precise mechanisms underlying histone methylation regulation are complex and require further elucidation.

Purpose of the Study:

  • To review current knowledge on the structural and biochemical aspects of histone recognition by specific protein domains.
  • To summarize the modes of interaction employed by Plant Homeodomain (PHD), Tudor, and Malignant Brain Tumor (MBT) domains with histone peptides.

Main Methods:

  • Literature review of structural and biochemical studies.
  • Analysis of protein-peptide interaction data for PHD, Tudor, and MBT domains.

Main Results:

  • Detailed structural insights into PHD, Tudor, and MBT domains.
  • Characterization of distinct recognition mechanisms for histone peptides by these domains.
  • Compilation of recent advancements in understanding histone modification recognition.

Conclusions:

  • PHD, Tudor, and MBT domains are critical readers of the histone code, interpreting methylation marks.
  • Structural and biochemical data are essential for understanding the specificity and function of these interactions.
  • Further research into these domains will illuminate epigenetic regulation and its role in disease.