Structure of nucleosome-bound human PBAF complex

Li Wang, Jiali Yu, Zishuo Yu, Qianmin Wang, Wanjun Li, Yulei Ren, Zhenguo Chen (), Shuang He () and Yanhui Xu ()
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Li Wang: Shanghai Medical College of Fudan University
Jiali Yu: Shanghai Medical College of Fudan University
Zishuo Yu: Shanghai Medical College of Fudan University
Qianmin Wang: Shanghai Medical College of Fudan University
Wanjun Li: Shanghai Medical College of Fudan University
Yulei Ren: Shanghai Medical College of Fudan University
Zhenguo Chen: Shanghai Medical College of Fudan University
Shuang He: Shanghai Medical College of Fudan University
Yanhui Xu: Shanghai Medical College of Fudan University

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract BAF and PBAF are mammalian SWI/SNF family chromatin remodeling complexes that possess multiple histone/DNA-binding subunits and create nucleosome-depleted/free regions for transcription activation. Despite previous structural studies and recent advance of SWI/SNF family complexes, it remains incompletely understood how PBAF-nucleosome complex is organized. Here we determined structure of 13-subunit human PBAF in complex with acetylated nucleosome in ADP-BeF3-bound state. Four PBAF-specific subunits work together with nine BAF/PBAF-shared subunits to generate PBAF-specific modular organization, distinct from that of BAF at various regions. PBAF-nucleosome structure reveals six histone-binding domains and four DNA-binding domains/modules, the majority of which directly bind histone/DNA. This multivalent nucleosome-binding pattern, not observed in previous studies, suggests that PBAF may integrate comprehensive chromatin information to target genomic loci for function. Our study reveals molecular organization of subunits and histone/DNA-binding domains/modules in PBAF-nucleosome complex and provides structural insights into PBAF-mediated nucleosome association complimentary to the recently reported PBAF-nucleosome structure.

Date: 2022
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DOI: 10.1038/s41467-022-34859-5

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