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TitleBasic helix-loop-helix pioneer factors interact with the histone octamer to invade nucleosomes and generate nucleosome-depleted regions.
Journal, issue, pagesMol Cell, Vol. 83, Issue 8, Page 1251-11263.e6, Year 2023
Publish dateApr 20, 2023
AuthorsBenjamin T Donovan / Hengye Chen / Priit Eek / Zhiyuan Meng / Caroline Jipa / Song Tan / Lu Bai / Michael G Poirier /
PubMed AbstractNucleosomes drastically limit transcription factor (TF) occupancy, while pioneer transcription factors (PFs) somehow circumvent this nucleosome barrier. In this study, we compare nucleosome binding ...Nucleosomes drastically limit transcription factor (TF) occupancy, while pioneer transcription factors (PFs) somehow circumvent this nucleosome barrier. In this study, we compare nucleosome binding of two conserved S. cerevisiae basic helix-loop-helix (bHLH) TFs, Cbf1 and Pho4. A cryo-EM structure of Cbf1 in complex with the nucleosome reveals that the Cbf1 HLH region can electrostatically interact with exposed histone residues within a partially unwrapped nucleosome. Single-molecule fluorescence studies show that the Cbf1 HLH region facilitates efficient nucleosome invasion by slowing its dissociation rate relative to DNA through interactions with histones, whereas the Pho4 HLH region does not. In vivo studies show that this enhanced binding provided by the Cbf1 HLH region enables nucleosome invasion and ensuing repositioning. These structural, single-molecule, and in vivo studies reveal the mechanistic basis of dissociation rate compensation by PFs and how this translates to facilitating chromatin opening inside cells.
External linksMol Cell / PubMed:36996811 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

25406

7ssa

EMDB-25406, PDB-7ssa:
Cryo-EM structure of pioneer factor Cbf1 bound to the nucleosome
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • xenopus laevis (African clawed frog)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
  • synthetic construct (others)
KeywordsGENE REGULATION / Transcription factor / basic helix-loop-helix / complex

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