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Michael, Alicia K.; Stoos, Lisa; Crosby, Priya; Eggers, Nikolas; Nie, Xinyu Y.; Makasheva, Kristina; Minnich, Martina; Healy, Kelly L.; Weiss, Joscha; Kempf, Georg; Cavadini, Simone; Kater, Lukas; Seebacher, Jan; Vecchia, Luca; Chakraborty, Deyasini; Isbel, Luke; Grand, Ralph S.; Andersch, Florian; Fribourgh, Jennifer L.; Schübeler, Dirk; Zuber, Johannes; Liu, Andrew C.; Becker, Peter B.; Fierz, Beat; [...]

Cooperation between bHLH transcription factors and histones for DNA access

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  • Medientyp: E-Artikel
  • Titel: Cooperation between bHLH transcription factors and histones for DNA access
  • Beteiligte: Michael, Alicia K.; Stoos, Lisa; Crosby, Priya; Eggers, Nikolas; Nie, Xinyu Y.; Makasheva, Kristina; Minnich, Martina; Healy, Kelly L.; Weiss, Joscha; Kempf, Georg; Cavadini, Simone; Kater, Lukas; Seebacher, Jan; Vecchia, Luca; Chakraborty, Deyasini; Isbel, Luke; Grand, Ralph S.; Andersch, Florian; Fribourgh, Jennifer L.; Schübeler, Dirk; Zuber, Johannes; Liu, Andrew C.; Becker, Peter B.; Fierz, Beat; [...]
  • Erschienen: Springer Science and Business Media LLC, 2023
  • Erschienen in: Nature
  • Sprache: Englisch
  • DOI: 10.1038/s41586-023-06282-3
  • ISSN: 1476-4687; 0028-0836
  • Entstehung:
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  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>The basic helix–loop–helix (bHLH) family of transcription factors recognizes DNA motifs known as E-boxes (CANNTG) and includes 108 members<jats:sup>1</jats:sup>. Here we investigate how chromatinized E-boxes are engaged by two structurally diverse bHLH proteins: the proto-oncogene MYC-MAX and the circadian transcription factor CLOCK-BMAL1 (refs. <jats:sup>2,3</jats:sup>). Both transcription factors bind to E-boxes preferentially near the nucleosomal entry–exit sites. Structural studies with engineered or native nucleosome sequences show that MYC-MAX or CLOCK-BMAL1 triggers the release of DNA from histones to gain access. Atop the H2A–H2B acidic patch<jats:sup>4</jats:sup>, the CLOCK-BMAL1 Per-Arnt-Sim (PAS) dimerization domains engage the histone octamer disc. Binding of tandem E-boxes<jats:sup>5–7</jats:sup> at endogenous DNA sequences occurs through direct interactions between two CLOCK-BMAL1 protomers and histones and is important for circadian cycling. At internal E-boxes, the MYC-MAX leucine zipper can also interact with histones H2B and H3, and its binding is indirectly enhanced by OCT4 elsewhere on the nucleosome. The nucleosomal E-box position and the type of bHLH dimerization domain jointly determine the histone contact, the affinity and the degree of competition and cooperativity with other nucleosome-bound factors.</jats:p>