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<p>Structural studies of nucleosomes most commonly involve histones from <i>Xenopus</i> 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 <i>LIN28B</i> 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 <i>Xenopus</i> histones.</p>

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Structural analysis of OCT4 binding to human LIN28B nucleosomes

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2026年1月19日

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  • Kalyan K. Sinha,
  • Mario Halic

摘要

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.