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Related Concept Videos

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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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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DNA in a human cell is almost 2m long and it is packed inside a tiny nucleus that is only a few microns in diameter. The level of compaction of DNA inside the nucleus is astonishing. It is organized into several sequentially higher levels of compaction to fit into such a tiny space. The most compact form of DNA is a chromosome that can be seen under a microscope in a dividing cell.
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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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Probing The Structure And Dynamics Of Nucleosomes Using Atomic Force Microscopy Imaging
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Structure of nucleosome-bound human BAF complex.

Shuang He1,2, Zihan Wu1,2, Yuan Tian1,2

  • 1Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering, and Shanghai Key Laboratory of Medical Epigenetics, Shanghai Medical College of Fudan University, Shanghai 200032, China.

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The study reveals the structure of the human BRG1/BRM-associated factor (BAF) complex bound to nucleosomes. This chromatin remodeler

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Mammalian SWI/SNF complexes, including BRG1/BRM-associated factor (BAF) and polybromo-associated BAF (PBAF), are crucial regulators of chromatin structure and gene transcription.
  • Dysfunctional SWI/SNF complexes, particularly BAF, are implicated in various human cancers due to mutations in their subunits.
  • Understanding the structural basis of BAF-nucleosome interaction is essential for deciphering its role in cellular processes and disease.

Purpose of the Study:

  • To elucidate the high-resolution structure of the human BAF complex bound to a nucleosome.
  • To provide detailed insights into the subunit organization and nucleosome recognition mechanisms of the BAF complex.
  • To identify key interactions between BAF subunits and the nucleosome, particularly focusing on cancer-associated mutations.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) was employed to determine the structure of the human BAF-nucleosome complex at 3.7 angstrom resolution.
  • Biochemical and structural analyses were performed to characterize the interactions between BAF subunits and nucleosomal DNA and histones.

Main Results:

  • The cryo-EM structure reveals the nucleosome is centrally positioned between the base and adenosine triphosphatase (ATPase) modules of the BAF complex, connected by the actin-related protein (ARP) module.
  • The ATPase motor is located near the nucleosomal DNA, facilitating DNA translocation along the nucleosome upon ATP hydrolysis.
  • The SMARCB1 subunit's C-terminal helix interacts with an acidic patch on the nucleosome, and this region is frequently mutated in cancers.
  • AT-rich interactive domain-containing protein 1A (ARID1A) and SMARCC form the structural core and scaffold of the BAF base module, respectively.

Conclusions:

  • The study provides unprecedented structural detail of the human BAF complex interacting with a nucleosome.
  • These findings illuminate the mechanisms by which BAF remodels chromatin and highlight the structural significance of cancer-associated mutations in subunits like SMARCB1.
  • The determined structure serves as a foundation for understanding BAF function in gene regulation and its role in oncogenesis.