ArticleNucleic acids research2017
PHF1 Tudor and N-terminal domains synergistically target partially unwrapped nucleosomes to increase DNA accessibility.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Molecular basis for PHF7-mediated ubiquitination of histone H3.Genes & development · 2023Article
- HIV-1 Preintegration Complex Preferentially Integrates the Viral DNA into Nucleosomes Containing Trimethylated Histone 3-Lysine 36 Modification and Flanking Linker DNA.Journal of virology · 2022Article
- Down-regulated m6A reader FTO destabilizes PHF1 that triggers enhanced stemness capacity and tumor progression in lung adenocarcinoma.Cell death discovery · 2022Article
- Quantifying epigenetic modulation of nucleosome breathing by high-throughput AFM imaging.Biophysical journal · 2022Article
- Evolutionary adaptation of the Polycomb repressive complex 2.Epigenetics & chromatin · 2022Review
- Mechanistic similarities in recognition of histone tails and DNA by epigenetic readers.Current opinion in structural biology · 2021Review
- Molecular mechanism of the MORC4 ATPase activation.Nature communications · 2020Article
- Nucleosome allostery in pioneer transcription factor binding.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- PHF1 fusions cause distinct gene expression and chromatin accessibility profiles in ossifying fibromyxoid tumors and mesenchymal cells.Modern pathology : an official journal of the United States and Canadian Academy of Pathology, Inc · 2020Article
- Ensembles of Breathing Nucleosomes: A Computational Study.Biophysical journal · 2020Article
- Molecular Basis for the PZP Domain of BRPF1 Association with Chromatin.Structure (London, England : 1993) · 2020Article
- Nonreciprocal and Conditional Cooperativity Directs the Pioneer Activity of Pluripotency Transcription Factors.Cell reports · 2019Article
- Understanding histone H3 lysine 36 methylation and its deregulation in disease.Cellular and molecular life sciences : CMLS · 2019Review
- Structural insights into the π-π-π stacking mechanism and DNA-binding activity of the YEATS domain.Nature communications · 2018Article
- Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome.eLife · 2018Article
- PHF1 is required for chromosome alignment and asymmetric division during mouse meiotic oocyte maturation.Cell cycle (Georgetown, Tex.) · 2018Article
- Recognition of cancer mutations in histone H3K36 by epigenetic writers and readers.Epigenetics · 2018Review
- The role of DNA sequence in nucleosome breathing.The European physical journal. E, Soft matter · 2017Article
- Covalent Modifications of Histone H3K9 Promote Binding of CHD3.Cell reports · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The Tudor domain of human PHF1 recognizes trimethylated lysine 36 on histone H3 (H3K36me3). PHF1 relies on this interaction to regulate PRC2 methyltransferase activity, localize to DNA double strand breaks and mediate nucleosome accessibility. Here, we investigate the impact of the PHF1 N-terminal domain (NTD) on the Tudor domain interaction with the nucleosome. We show that the NTD is partially ordered when it is natively attached to the Tudor domain. Through a combination of FRET and single molecule studies, we find that the increase of DNA accessibility within the H3K36me3-containing nucleosome, instigated by the Tudor binding to H3K36me3, is dramatically enhanced by the NTD. We demonstrate that this nearly order of magnitude increase is due to preferential binding of PHF1 to partially unwrapped nucleosomes, and that PHF1 alters DNA-protein binding within the nucleosome by decreasing dissociation rates. These results highlight the potency of a PTM-binding protein to regulate DNA accessibility and underscores the role of the novel mechanism by which nucleosomes control DNA-protein binding through increasing protein dissociation rates.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.