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Related Concept Videos

Histone Modification02:32

Histone Modification

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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
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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.
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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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Nucleosome Remodeling02:54

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Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
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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.
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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.
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Deciphering Molecular Mechanism of Histone Assembly by DNA Curtain Technique
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Structural insights into histone exchange by human SRCAP complex.

Jiali Yu1,2, Fengrui Sui1, Feng Gu1

  • 1Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, New Cornerstone Science Laboratory, State Key Laboratory of Genetic Engineering and Shanghai Key Laboratory of Medical Epigenetics, Shanghai Medical College of Fudan University, Shanghai, China.

Cell Discovery
|February 8, 2024
PubMed
Summary
This summary is machine-generated.

The SRCAP complex (SRCAP-C) replaces histone H2A with H2A.Z at promoters to regulate transcription. Structural studies reveal how SRCAP-C destabilizes and removes H2A-H2B dimers, facilitating H2A.Z incorporation.

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Area of Science:

  • Chromatin biology
  • Molecular mechanisms of transcription regulation
  • Structural biology

Background:

  • Histone variant H2A.Z is crucial for gene transcription regulation.
  • The SRCAP complex (SRCAP-C) facilitates the exchange of canonical H2A-H2B dimers with H2A.Z-H2B dimers.
  • Understanding the structural basis of this exchange is key to deciphering transcriptional control.

Purpose of the Study:

  • To determine the near-atomic resolution structures of human SRCAP-C bound to H2A-containing nucleosomes.
  • To elucidate the molecular mechanism by which SRCAP-C mediates H2A-H2A.Z exchange.

Main Methods:

  • Near-atomic resolution cryo-electron microscopy (cryo-EM) of human SRCAP-C bound to nucleosomes.
  • Biochemical assays to study ATPase activity and nucleosome binding modes.
  • Structure-guided chromatin immunoprecipitation sequencing (ChIP-seq) to assess genomic H2A.Z occupancy.

Main Results:

  • The SRCAP subunit comprises an actin-related protein (ARP) module and an ATPase motor module.
  • The ARP module encircles nucleosomal DNA, potentially restraining DNA translocation.
  • Distinct binding modes of the motor module in different nucleotide-bound states reveal an ATPase-driven mechanism that destabilizes and extracts H2A-H2B via the ZNHIT1 subunit.
  • Structure-guided ChIP-seq confirmed ZNHIT1's role in maintaining H2A.Z genomic occupancy.

Conclusions:

  • The study provides unprecedented structural insights into the H2A-H2A.Z exchange mechanism mediated by SRCAP-C.
  • The findings illuminate how SRCAP-C utilizes ATPase activity to remodel nucleosomes and regulate transcription.
  • ZNHIT1 is identified as a critical component for H2A.Z maintenance on the genome.