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Related Concept Videos

Histone Modification02:32

Histone Modification

13.4K
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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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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Heterochromatin02:38

Heterochromatin

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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...
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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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Chromatin Modification in iPS Cells01:32

Chromatin Modification in iPS Cells

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Chromatin modification alters gene expression; therefore, scientists can add histone-modifying enzymes, histone variants, and chromatin remodeling complexes to somatic cells to aid reprogramming into pluripotent stem (iPS) cells.
Compact chromatin makes reprogramming difficult. Enzymes, such as histone demethylases and acetyltransferases, are often added during reprogramming to loosen the chromatin, making the DNA more accessible to transcription factors. Molecules that inhibit histone...
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Histone Variants at the Centromere02:30

Histone Variants at the Centromere

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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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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Two assembly modes for SIN3 histone deacetylase complexes.

Chengcheng Wang1,2,3, Zhouyan Guo4,5,6, Chen Chu4,5,6

  • 1Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China. wangchengcheng@westlake.edu.cn.

Cell Discovery
|April 19, 2023
PubMed
Summary
This summary is machine-generated.

The study reveals distinct structures of SIN3/histone deacetylase (HDAC) complexes in yeast, uncovering two assembly mechanisms that regulate gene expression and chromatin accessibility.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Epigenetics

Background:

  • Switch-independent 3 (SIN3)/histone deacetylase (HDAC) complexes are crucial for gene regulation.
  • Two main types, SIN3L and SIN3S, target distinct genomic regions.

Purpose of the Study:

  • To determine the cryo-electron microscopy structures of SIN3L and SIN3S complexes from Schizosaccharomyces pombe.
  • To elucidate the distinct assembly mechanisms and structural features of these complexes.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was used to resolve the structures.
  • Structural analysis focused on the subunit interactions and overall complex organization.

Main Results:

  • SIN3L and SIN3S complexes exhibit two unique assembly modes.
  • SIN3L forms a two-lobed structure with Sin3 isoforms (Pst1, Pst3), Clr6, and Prw1, bridged by Sds3/Dep1 and Rxt2/Png2.
  • SIN3S forms a single lobe with Sin3 isoform Pst2, Cph1/Cph2, and Eaf3, featuring histone-binding modules.

Conclusions:

  • The findings reveal distinct structural mechanisms for SIN3/HDAC complex organization.
  • These mechanisms enable specific targeting and function in chromatin regulation.
  • Provides a structural framework for understanding histone deacetylase complex assembly and function.