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    Spatiotemporal dynamics of 53BP1 dimer recruitment to a DNA double strand break

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    Author
    Lou, J; Priest, DG; Solano, A; Kerjouan, A; Hinde, E
    Date
    2020-11-13
    Source Title
    Nature Communications
    Publisher
    NATURE RESEARCH
    University of Melbourne Author/s
    Hinde, Elizabeth
    Affiliation
    School of Physics
    Metadata
    Show full item record
    Document Type
    Journal Article
    Citations
    Lou, J., Priest, D. G., Solano, A., Kerjouan, A. & Hinde, E. (2020). Spatiotemporal dynamics of 53BP1 dimer recruitment to a DNA double strand break. NATURE COMMUNICATIONS, 11 (1), https://doi.org/10.1038/s41467-020-19504-3.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/253031
    DOI
    10.1038/s41467-020-19504-3
    Open Access at PMC
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7666136
    Abstract
    Tumor suppressor p53-binding protein 1 (53BP1) is a DNA repair protein essential for the detection, assessment, and resolution of DNA double strand breaks (DSBs). The presence of a DSB is signaled to 53BP1 via a local histone modification cascade that triggers the binding of 53BP1 dimers to chromatin flanking this type of lesion. While biochemical studies have established that 53BP1 exists as a dimer, it has never been shown in a living cell when or where 53BP1 dimerizes upon recruitment to a DSB site, or upon arrival at this nuclear location, how the DSB histone code to which 53BP1 dimers bind regulates retention and self-association into higher-order oligomers. Thus, here in live-cell nuclear architecture we quantify the spatiotemporal dynamics of 53BP1 oligomerization during a DSB DNA damage response by coupling fluorescence fluctuation spectroscopy (FFS) with the DSB inducible via AsiSI cell system (DIvA). From adopting this multiplexed approach, we find that preformed 53BP1 dimers relocate from the nucleoplasm to DSB sites, where consecutive recognition of ubiquitinated lysine 15 of histone 2A (H2AK15ub) and di-methylated lysine 20 of histone 4 (H4K20me2), leads to the assembly of 53BP1 oligomers and a mature 53BP1 foci structure.

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