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Structures and implications of TBP-nucleosome complexes.

Haibo Wang1, Le Xiong1, Patrick Cramer2

  • 1Department of Molecular Biology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany.

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|July 24, 2021
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Summary

TATA box-binding protein (TBP) binds to nucleosomes, with TFIIA stabilizing this interaction. TBP-nucleosome binding prevents transcription preinitiation complex assembly, explaining how nucleosomes impede gene activation.

Keywords:
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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • TATA box-binding protein (TBP) is crucial for transcription initiation.
  • TBP facilitates transcription preinitiation complex (PIC) assembly at gene promoters.
  • Nucleosomes can impede PIC assembly and transcription.

Purpose of the Study:

  • To investigate the interaction between yeast TBP and nucleosomes.
  • To determine the structural basis of TBP-nucleosome binding.
  • To understand how TBP-nucleosome interactions affect PIC assembly.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine complex structures.
  • Biochemical assays to study TBP-nucleosome binding.
  • Analysis of TBP binding sites on nucleosomal DNA.

Main Results:

  • Yeast TBP binds to nucleosomes containing the Widom-601 sequence.
  • TFIIA stabilizes TBP-nucleosome binding.
  • TBP binds at superhelical locations (SHL) -6 and +2 on the nucleosome.
  • Binding at SHL +2, dependent on TFIIA, causes DNA detachment from histones.
  • TBP-nucleosome complexes are sterically incompatible with PIC assembly.

Conclusions:

  • Nucleosomes containing TBP and TFIIA are structurally incompatible with transcription initiation.
  • TBP-nucleosome interactions provide a mechanism for how promoter nucleosomes inhibit transcription.
  • Nucleosome repositioning is likely required for transcription initiation at repressed genes.