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Related Concept Videos

The Nucleosome02:33

The Nucleosome

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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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Human DNA is almost two meters long. However, it is compressed inside a tiny nucleus measuring only a few microns in diameter. To make this degree of compaction possible, DNA is organized into several sequential levels so that it can 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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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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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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Structural basis for BCL7B-mediated ncBAF-nucleosome engagement.

Fahui Sun1, Binqian Zou2, He Li3

  • 1State Key Laboratory of Respiratory Disease, Center for Biomedical Digital Science, GIBH-CUHK Joint Research Laboratory on Stem Cell and Regenerative Medicine, Guangdong Provincial Key Laboratory of Stem Cell and Regenerative Medicine, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.

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This summary is machine-generated.

The study reveals how non-canonical BAF (ncBAF) chromatin remodelers interact with nucleosomes, identifying BCL7 proteins as key tethers. This work clarifies ncBAF

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Area of Science:

  • Molecular Biology
  • Chromatin Biology
  • Structural Biology

Background:

  • Mammalian SWI/SNF complexes (cBAF, PBAF, ncBAF) remodel nucleosomes using ATP hydrolysis.
  • The chromatin interaction mechanisms of cBAF and PBAF are known, but ncBAF remains uncharacterized.
  • Understanding ncBAF structure is crucial for elucidating its role in gene regulation.

Purpose of the Study:

  • To resolve the molecular architecture of ncBAF-nucleosome complexes.
  • To understand the role of BCL7 proteins in ncBAF chromatin engagement.
  • To investigate the functional implications of ncBAF's interaction with nuclear actin filaments.

Main Methods:

  • Integration of cryo-electron microscopy (cryo-EM).
  • Biochemical assays.
  • Cross-linking mass spectrometry (XL-MS).

Main Results:

  • The conformational transition of ncBAF-nucleosome complexes from nucleotide-free to nucleotide-bound states was resolved.
  • BCL7 proteins act as dynamic tethers linking the ARP module to the nucleosomal acidic patch.
  • BCL7B enhances ncBAF-mediated remodeling, and β-actin within the ARP module retains ATP hydrolysis activity, potentially linking to nuclear actin networks.

Conclusions:

  • BCL7 plays a dynamic role in regulating ncBAF-mediated chromatin remodeling.
  • ncBAF exhibits a distinct chromatin engagement mode compared to cBAF/PBAF.
  • The findings provide a molecular basis for coordinating nuclear actin with chromatin remodeling.