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Preparation of Nucleosome Core Particles Complexed with DNA Repair Factors for Cryo-Electron Microscopy Structural Determination
Published on: August 17, 2022
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Structure of nucleosome-bound human PBAF complex.
Li Wang1,2,3, Jiali Yu1, Zishuo Yu1
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.
Nature Communications
|December 10, 2022
Summary
The study reveals the molecular organization of the PBAF chromatin remodeling complex bound to a nucleosome. This detailed structure highlights PBAF
Area of Science:
- Molecular biology
- Chromatin biology
- Structural biology
Background:
- Mammalian SWI/SNF complexes, including BAF and PBAF, remodel chromatin for transcription.
- The precise organization of the PBAF-nucleosome complex remains incompletely understood.
Purpose of the Study:
- To determine the structure of the 13-subunit human PBAF complex in association with an acetylated nucleosome.
- To elucidate the molecular organization and subunit interactions within the PBAF-nucleosome complex.
Main Methods:
- X-ray crystallography to determine the structure of the PBAF-nucleosome complex.
- Biochemical assays to characterize subunit interactions and binding domains.
Main Results:
- Detailed structure of the 13-subunit human PBAF complex bound to an acetylated nucleosome.
- Identification of PBAF-specific modular organization distinct from BAF.
- Revealed six histone-binding and four DNA-binding domains/modules involved in multivalent nucleosome binding.
Conclusions:
- The PBAF-nucleosome structure provides insights into the complex's molecular organization and subunit interactions.
- Multivalent nucleosome binding suggests PBAF integrates chromatin information for targeted genomic functions.
- Structural data complements previous findings on PBAF-nucleosome association.
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