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TitleStructural analysis of OCT4 binding to human LIN28B nucleosomes.
Journal, issue, pagesSci Rep, Vol. 16, Issue 1, Page 5704, Year 2026
Publish dateJan 19, 2026
AuthorsKalyan K Sinha / Mario Halic /
PubMed AbstractStructural studies of nucleosomes most commonly involve histones from Xenopus species or humans. Yet, the effect of subtle differences in the amino acid sequences of these histones on key aspects of ...Structural studies of nucleosomes most commonly involve histones from Xenopus species or humans. Yet, the effect of subtle differences in the amino acid sequences of these histones on key aspects of structure, such as nucleosome assembly, DNA positioning, and transcription factor binding remains unclear. Here, we show that histones from both species can efficiently assemble on the human LIN28B DNA sequence. Using cryogenic electron microscopy we demonstrate that the pioneer transcription factor OCT4 engages with LIN28B nucleosomes assembled with human histones in the same manner as observed in our previous work in which the nucleosomes were assembled with Xenopus histones.
External linksSci Rep / PubMed:41554871 / PubMed Central
MethodsEM (single particle)
Resolution6.0 Å
Structure data

EMDB-72371: Human Oct4 bound to nucleosome reconstituted with human histones and 182 bp human LIN28B sequence
Method: EM (single particle) / Resolution: 6.0 Å

Source
  • Homo sapiens (human)

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