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FOXP3 recognizes microsatellites and bridges DNA through multimerization.

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FOXP3 protein forms higher-order multimers on microsatellites, revealing a novel DNA recognition mechanism. This finding clarifies FOXP3

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Area of Science:

  • Molecular Biology
  • Immunology
  • Genetics

Background:

  • FOXP3 is crucial for regulatory T cell development, controlling inflammation and autoimmunity.
  • The precise molecular mechanisms of FOXP3 function remain largely unknown.
  • Understanding FOXP3's DNA binding is key to its role in immune regulation.

Purpose of the Study:

  • To elucidate the molecular mechanisms of FOXP3's DNA binding and transcriptional regulation.
  • To investigate how FOXP3 interacts with microsatellite DNA sequences.
  • To determine the structural basis of FOXP3's function in regulatory T cells.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine the structure of FOXP3-DNA complexes.
  • Site-directed mutagenesis to assess the functional importance of FOXP3 domains.
  • In vitro and cellular assays to evaluate DNA binding and regulatory T cell function.

Main Results:

  • FOXP3 forms higher-order multimers on TnG repeat microsatellites, adopting a ladder-like architecture.
  • The forkhead domain mediates this multimerization, bridging DNA molecules.
  • Mutations affecting multimerization impair DNA recognition and cellular functions without affecting consensus motif binding.
  • FOXP3 exhibits broad specificity for TnG-like sequences due to flexible inter-rung spacing.

Conclusions:

  • FOXP3 utilizes a novel DNA recognition mode involving homomultimerization and DNA bridging on microsatellites.
  • Microsatellites play a significant role in transcriptional regulation and disease pathogenesis.
  • This discovery provides new insights into the molecular basis of immune regulation and autoimmune diseases.