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Related Concept Videos

Histone Modification02:32

Histone Modification

16.2K
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

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Histone Variants at the Centromere02:30

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Histone variants are the histone proteins with structural and sequence variations. These variants may be regarded as “mutant” forms that replace their canonical histone counterparts in the nucleosomes. Specific post-translational modifications on the histone variants enable further chromatin complexity and regulate tissue-specific gene expression. The most common histone variants are from histone H2A, H2B, and linker histone H1 families. However, several variants of histone H3...
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Spreading of Chromatin Modifications02:25

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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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Chromatin Packaging02:21

Chromatin Packaging

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Each human somatic cell contains 6 billion base-pairs of DNA. Each base-pair is 0.34 nm long, which means that each diploid cell contains a staggering 2 meters of DNA. How is such a long DNA strand packed inside a nucleus measuring only 10 - 20 microns in diameter? 
The chromatin
In combination with specialized DNA binding protein called Histones, the DNA double helix forms a compact DNA: protein complex called chromatin. The chromatin itself is further compacted into higher-order...
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Chromatin Packaging01:32

Chromatin Packaging

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Each human somatic cell contains 6 billion base pairs of DNA. Each base pair is 0.34 nm long, meaning each diploid cell contains a staggering 2 meters of DNA. This long DNA strand is packed inside a nucleus measuring only 10-20 microns in diameter with the help of specialized DNA-binding proteins called histones. Together they form a compact DNA-protein complex called chromatin. The chromatin is further compacted into higher-order structures. The highest level of compaction is achieved during...
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Sequential Salt Extractions for the Analysis of Bulk Chromatin Binding Properties of Chromatin Modifying Complexes
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Modifying Chromatin by Histone Tail Clipping.

Gajendra Kumar Azad1, Swati Swagatika2, Manoj Kumawat2

  • 1Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore.

Journal of Molecular Biology
|July 17, 2018
PubMed
Summary
This summary is machine-generated.

Histone post-translational modifications (PTMs) regulate gene expression and cellular processes. This review highlights histone clipping, a conserved epigenetic mechanism, and its role in biological functions.

Keywords:
chromatinchromatin dynamicschromatin-modifying enzymeshistone clippinghistone-specific proteases

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Area of Science:

  • Epigenetics
  • Molecular Biology
  • Biochemistry

Background:

  • Histone post-translational modifications (PTMs) are vital for regulating chromatin structure and cellular functions like DNA replication, repair, and transcription.
  • Chromatin modifiers dynamically regulate histone PTMs, which are recognized by reader proteins to control gene expression.
  • Dysregulation of histone PTMs can lead to cellular defects and various diseases.

Purpose of the Study:

  • To review the significance of histone clipping as a conserved epigenetic phenomenon.
  • To explore the regulatory roles of histone clipping in biological processes.
  • To identify future research directions for understanding histone clipping mechanisms.

Main Methods:

  • Literature review of studies on histone modifications and epigenetic regulation.
  • Analysis of research on histone clipping across different species.
  • Synthesis of current knowledge on the interplay between histone PTMs, chromatin dynamics, and cellular functions.

Main Results:

  • Histone clipping is a conserved epigenetic mechanism observed from yeast to mammals.
  • Proteolytic clipping of histones influences various biological processes.
  • The interplay between histone PTMs and chromatin dynamics is crucial for cellular regulation.

Conclusions:

  • Histone clipping represents a distinct and understudied epigenetic event with significant biological implications.
  • Further research is needed to fully elucidate the mechanisms and functions of histone clipping.
  • Understanding histone clipping may offer new insights into disease pathogenesis and therapeutic strategies.