Structure of nucleosome-bound human PBAF complex

• Published in: Nature communications Vol. 13; no. 1; p. 7644
• Main Authors: Wang, Li, Yu, Jiali, Yu, Zishuo, Wang, Qianmin, Li, Wanjun, Ren, Yulei, Chen, Zhenguo, He, Shuang, Xu, Yanhui
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 10.12.2022; Nature Publishing Group UK; Nature Portfolio
• Subjects: Adenosine diphosphate; Adenosine triphosphate; Animals; Binding; Chromatin Assembly and Disassembly; Chromatin remodeling; Chromosomal Proteins, Non-Histone - metabolism; Deoxyribonucleic acid; Depletion; DNA; Domains; Epigenetics; Histones; Histones - genetics; Histones - metabolism; Humans; Information processing; Laboratories; Mammals - genetics; Mass spectrometry; Modular structures; Modules; Nucleosomes - genetics; Scientific imaging; Transcription activation; Transcription Factors - metabolism
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-022-34859-5

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-BeF -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.