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FoxP3 recognizes microsatellites and bridges DNA through multimerization.

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    FoxP3, crucial for regulatory T cells, forms higher-order multimers on microsatellites, revealing a novel DNA binding mechanism. This discovery impacts understanding of transcriptional regulation and diseases.

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    Area of Science:

    • Molecular biology
    • Structural biology
    • Immunology

    Background:

    • FoxP3 is a transcription factor vital for regulatory T cell (Treg) development, which are critical for immune homeostasis.
    • The precise molecular mechanisms governing FoxP3 function, particularly its DNA binding, remain incompletely understood.

    Approach:

    • Utilized cryo-electron microscopy to determine the structure of FoxP3 bound to TnG repeat microsatellites.
    • Investigated the role of specific interfaces within the FoxP3 multimer through mutational analysis.
    • Assessed the impact of mutations on DNA recognition, DNA bridging, and cellular functions.

    Key Points:

    • FoxP3 forms higher-order multimers on TnG repeat microsatellites, a previously unrecognized mode of DNA binding.
    • The cryo-EM structure reveals a ladder-like architecture with FoxP3 pairs forming "rungs" bridging DNA "side rails".
    • Mutations disrupting the "intra-rung" interface impair microsatellite recognition and DNA bridging, but not binding to the canonical Forkhead consensus motif.

    Conclusions:

    • Reveals a novel DNA recognition mechanism involving transcription factor homo-multimerization and DNA bridging.
    • Suggests that microsatellites play a significant role in transcriptional regulation.
    • Provides insights into potential mechanisms underlying diseases associated with FoxP3 dysfunction.