Structure of nucleosome-bound human PBAF complex.
Structure of nucleosome-bound human PBAF complex.
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DOI:
10.1038/s41467-022-34859-5
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发表时间:
2022-12-10
影响因子:
16.6
通讯作者:
Xu, Yanhui
中科院分区:
文献类型:
--
作者:
Wang, Li;Yu, Jiali;Yu, Zishuo;Wang, Qianmin;Li, Wanjun;Ren, Yulei;Chen, Zhenguo;He, Shuang;Xu, Yanhui
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. BAF and PBAF are SWI/SNF family chromatin remodeling complexes that create nucleosome-depleted regions for transcription activation. Here the authors report the structure of a 13-subunit human PBAF in complex with acetylated nucleosome in ADP-BeF3-bound state that provides structural insights into PBAF-mediated nucleosome association.
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