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Related Concept Videos

Histone Modification02:32

Histone Modification

15.1K
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...
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Histone Modification02:32

Histone Modification

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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...
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The Nucleosome Core Particle01:12

The Nucleosome Core Particle

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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...
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The Nucleosome Core Particle02:10

The Nucleosome Core Particle

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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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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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

Bethany C Taylor1, Nicolas L Young1,2

  • 1Verna & Marrs McLean Department of Biochemistry & Molecular Biology, Baylor College of Medicine, Houston, TX, U.S.A.

The Biochemical Journal
|February 10, 2021
PubMed
Summary

Histone post-translational modifications (PTMs) regulate the genome. Combinations of these histone PTMs act as the central mechanism for chromatin-mediated genome regulation, with reader proteins interpreting these signals.

Keywords:
chromatinhistonespost-translational modificationproteomics

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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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Author Spotlight: Enhanced Histone PTM Isomer Identification Through LC-TIMS-ToF MS/MS and PASEF
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Area of Science:

  • Molecular Biology
  • Genetics
  • Epigenetics

Background:

  • Histones are key proteins for eukaryotic genome packaging into nucleosomes, chromatin, and chromosomes.
  • Histone post-translational modifications (PTMs) are vital for dynamic and persistent genome regulation.
  • Histone PTMs convey complex genomic state signals through combinatorial patterns.

Purpose of the Study:

  • To review the combinatorial functions of histone PTMs.
  • To assess methods for measuring combinatorial PTMs.
  • To provide a reference for investigating PTM functions and discovering new synergies.

Main Methods:

  • Literature review of histone PTMs and their reader proteins.
  • Analysis of existing methodologies for detecting combinatorial histone PTMs.
  • Discussion of the functional implications of PTM combinations.

Main Results:

  • Histone PTMs function combinatorially to regulate the genome.
  • Reader proteins are crucial for transducing signals from PTMs.
  • Current methods have limitations in measuring complex PTM patterns.

Conclusions:

  • Combinations of histone PTMs are central to chromatin-mediated genome regulation.
  • Further research is needed to fully understand combinatorial PTM functions.
  • Investigating PTM synergies is essential for advancing epigenetics research.