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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,...
Duplication of Chromatin Structure02:05

Duplication of Chromatin Structure

The process of chromosome duplication during cell division requires genome-wide disruption and re-assembly of chromatin. The chromatin structure must be accurately inherited, reassembled, and maintained in the daughter cells to ensure lineage propagation.
The basic unit of the chromatin is the nucleosome, consisting of DNA wrapped around octameric histone proteins and short stretches of linker DNA separating individual nucleosomes. The histone proteins within the nucleosome have their...
Chromatin Packaging01:32

Chromatin Packaging

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...
Chromatin Packaging02:21

Chromatin Packaging

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 structures.
Chromatin Packaging02:21

Chromatin Packaging

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 structures.

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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique

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Combinatorial complexity in chromatin structure and function: revisiting the histone code.

Oliver J Rando1

  • 1Department of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, MA 01605, USA. oliver.rando@umassmed.edu

Current Opinion in Genetics & Development
|March 24, 2012
PubMed
Summary
This summary is machine-generated.

Histone modifications regulate gene expression and DNA repair. This review explores the debate around the histone code hypothesis, examining evidence for and against combinatorial histone mark functions.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Genetics

Background:

  • Covalent modifications of histone proteins are crucial for fundamental cellular processes like transcription, DNA repair, and recombination.
  • Over 100 distinct histone modifications have been identified, influencing chromatin structure and function.
  • The 'histone code hypothesis' proposes that the biological outcome of a histone mark depends on its combination with other marks.

Purpose of the Study:

  • To review the contrasting evidence regarding the combinatorial nature of histone modifications.
  • To discuss the implications of these findings for understanding gene regulation.
  • To explore potential resolutions for the discrepancies between biochemical and functional studies.

Main Methods:

  • Literature review of biochemical, functional, and localization studies on histone modifications.
  • Analysis of evidence supporting and refuting the histone code hypothesis.
  • Discussion of chromatin regulatory factors and their interaction with histone marks.

Main Results:

  • Biochemical studies show chromatin regulatory factors binding to specific histone modification combinations.
  • Functional and localization studies indicate limited combinatorial complexity in actual histone modification patterns.
  • Conflicting data exists regarding the extent of combinatorial regulation by histone marks.

Conclusions:

  • The precise role and complexity of combinatorial histone modifications remain a subject of active debate.
  • Reconciling biochemical and functional evidence is key to advancing our understanding of epigenetics.
  • Further research is needed to elucidate the functional significance of histone mark combinations in vivo.