ArticleScientific reports2020
Nucleosome binding by the pioneer transcription factor OCT4.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 55 citations in OpenAlex.
- H2A.Z facilitates Sox2-nucleosome interaction by promoting DNA and histone H3 tail mobility.Nucleic acids research · 2026Article
- Structural analysis of OCT4 binding to human LIN28B nucleosomes.Scientific reports · 2026Article
- DNA bendability regulates transcription factor binding to nucleosomes.Nature structural & molecular biology · 2025Article
- Native nucleosome-positioning elements as alternatives to the 601 sequence for nucleosome repositioning studies.Nucleic acids research · 2025Article
- Structural insights into the recognition of native nucleosomes by pioneer transcription factors.Current opinion in structural biology · 2025Review
- The maternal-to-zygotic transition: reprogramming of the cytoplasm and nucleus.Nature reviews. Genetics · 2025Review
- Mesoscale chromatin confinement facilitates target search of pioneer transcription factors in live cells.Nature structural & molecular biology · 2025Article
- Rise and SINE: roles of transcription factors and retrotransposons in zygotic genome activation.Nature reviews. Molecular cell biology · 2025Article
- Structural insights into the cooperative nucleosome recognition and chromatin opening by FOXA1 and GATA4.Molecular cell · 2024Article
- Exploring the reciprocity between pioneer factors and development.Development (Cambridge, England) · 2024Review
- Structural dynamics in chromatin unraveling by pioneer transcription factors.Biophysical reviews · 2024Review
- Structural mechanism of synergistic targeting of the CX3CR1 nucleosome by PU.1 and C/EBPα.Nature structural & molecular biology · 2024Article
- Pioneer factors: roles and their regulation in development.Trends in genetics : TIG · 2024Review
- Article
- Structural mechanism of LIN28B nucleosome targeting by OCT4.Molecular cell · 2023Article
- Histone modifications regulate pioneer transcription factor binding and cooperativity.bioRxiv : the preprint server for biology · 2023Article
- Epigenetic Regulation of Driver Genes in Testicular Tumorigenesis.International journal of molecular sciences · 2023Review
- Till SMARCA5 loss do nucleosomes part.Molecular cell · 2023Article
- Structural Plasticity of Pioneer Factor Sox2 and DNA Bendability Modulate Nucleosome Engagement and Sox2-Oct4 Synergism.Journal of molecular biology · 2023Article
- Structural mechanism ofbioRxiv : the preprint server for biology · 2023Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription factor binding to genomic DNA is generally prevented by nucleosome formation, in which the DNA is tightly wrapped around the histone octamer. In contrast, pioneer transcription factors efficiently bind their target DNA sequences within the nucleosome. OCT4 has been identified as a pioneer transcription factor required for stem cell pluripotency. To study the nucleosome binding by OCT4, we prepared human OCT4 as a recombinant protein, and biochemically analyzed its interactions with the nucleosome containing a natural OCT4 target, the LIN28B distal enhancer DNA sequence, which contains three potential OCT4 target sequences. By a combination of chemical mapping and cryo-electron microscopy single-particle analysis, we mapped the positions of the three target sequences within the nucleosome. A mutational analysis revealed that OCT4 preferentially binds its target DNA sequence located near the entry/exit site of the nucleosome. Crosslinking mass spectrometry consistently showed that OCT4 binds the nucleosome in the proximity of the histone H3 N-terminal region, which is close to the entry/exit site of the nucleosome. We also found that the linker histone H1 competes with OCT4 for the nucleosome binding. These findings provide important information for understanding the molecular mechanism by which OCT4 binds its target DNA in chromatin.
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