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    Home > Biochemistry News > Biotechnology News > The latest article published by Peking University's Nature: Unraveling the structure of human PBAF chromatin remodeling complex bound to nucleosomes

    The latest article published by Peking University's Nature: Unraveling the structure of human PBAF chromatin remodeling complex bound to nucleosomes

    • Last Update: 2022-05-13
    • Source: Internet
    • Author: User
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    On April 27, 2022, the Joint Center for Life Sciences, the School of Life Sciences of Tsinghua University, the Advanced Innovation Center for Structural Biology, Zhucheng Chen, and the research team published online in the journal Nature entitled "Human-derived PBAF chromatin remodeling complex.



    In eukaryotes, DNA is wrapped around histones to form nucleosomes, which are highly compressed to form chromatin



    BAF (BRG1-associated factors) and PBAF (polybromo-associated BRG1-associated factors) are chromatin remodeling complexes of the mammalian SWI/SNF family, they regulate chromatin structure and gene expression, and are widely involved in the development and differentiation of animal cells



    Chen Zhucheng's research team has been deeply involved in the field of chromatin remodeling for a long time and has published a series of important results



    The 12 subunits of the PBAF complex can be divided into three modules according to their different functions: the motor module with catalytic activity, the ARP (actin-related protein) module with regulatory functions, and the SRM module (substrate) with chromatin targeting functions.


    Notably, the motor subunit SMARCA4 is active in the complex resolved in this study


    In conclusion, this work not only elucidates the mechanisms of PBAF complex assembly, nucleosome recognition, and chromatin remodeling, but also provides a theoretical basis for understanding the pathogenic mechanisms of BAF/PBAF-related mutations


    Chen Zhu became the corresponding author of this article


     

    Original link:

     https:// 

     Structure and disease-associated mutations of the PBAF chromatin remodeling complex bound to nucleosomes 

    (a) Cryo-EM density map of PBAF-nucleosome complexes



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