ArticleEpigenetics & chromatin2020
Characterization of the plant homeodomain (PHD) reader family for their histone tail interactions.
Article in Epigenetics & chromatin, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Tandem bromodomains of BRD4 cooperatively read poly-acetylated nucleosomes to enhance chromatin engagement and regulate breast cancer phenotypes.bioRxiv : the preprint server for biology · 2026Article
- Article
- Direct Readout of Multivalent Chromatin Reader-Nucleosome Interactions by Nucleosome Mass Spectrometry.ACS central science · 2026Article
- Myositis-specific autoantibodies recognising Mi2 also target the AIRE protein at a shared PHD zinc finger.Annals of the rheumatic diseases · 2026Article
- Genome-wide identification and characterization of SET domain family genes in Neopyropia yezoensis.BMC genomics · 2026Article
- Current insights into PHF14: molecular features and functional roles.Frontiers in molecular biosciences · 2026Review
- Anti-Mi2 autoantibodies target PHD fingers of SP140L and TIF1γ, while anti-TIF1γ autoantibodies primarily bind TIF1γ outside the PHD region.Rheumatology (Oxford, England) · 2025Article
- Interferon dependent immune memory during HSV-1 neuronal latency via increased H3K9me3 and restriction by ATRX.Nature communications · 2025Article
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- A novel heterozygous pathogenicJournal of human immunity · 2025Article
- Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains.Nucleic acids research · 2025Article
- Article
- Deciphering the molecular mechanisms of BPTF interactions with nucleosomes via molecular simulations.Biophysical journal · 2025Article
- Histone H3 N-terminal recognition by the PHD finger of PHRF1 is required for proper DNA damage response.Nucleic acids research · 2025Article
- Deciphering the Molecular Mechanisms of BPTF Interactions with Nucleosomes via Molecular Simulations.bioRxiv : the preprint server for biology · 2025Article
- Anti-Mi2 autoantibodies target the PHD fingers of SP140L and TIF1γ, while anti-TIF1γ autoantibodies primarily recognize epitopes outside the PHD region of TIF1γ.medRxiv : the preprint server for health sciences · 2025Article
- A LANA peptide inhibits tumor growth by inducing CHD4 protein cleavage and triggers cell death.Cell chemical biology · 2024Article
- PHF10 inhibits gastric epithelium differentiation and induces gastric cancer carcinogenesis.Cancer gene therapy · 2024Article
- Mechanism for controlled assembly of transcriptional condensates by Aire.Nature immunology · 2024Article
- The Role of Tripartite Motif Family Proteins in Chronic Liver Diseases: Molecular Mechanisms and Therapeutic Potential.Biomolecules · 2024Review
2 more citing papers are in PubMed but not listed here.
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Authors and funding
14 authors.
Funding
Abstract
backgroundPlant homeodomain (PHD) fingers are central "readers" of histone post-translational modifications (PTMs) with > 100 PHD finger-containing proteins encoded by the human genome. Many of the PHDs studied to date bind to unmodified or methylated states of histone H3 lysine 4 (H3K4). Additionally, many of these domains, and the proteins they are contained in, have crucial roles in the regulation of gene expression and cancer development. Despite this, the majority of PHD fingers have gone uncharacterized; thus, our understanding of how these domains contribute to chromatin biology remains incomplete.
resultsWe expressed and screened 123 of the annotated human PHD fingers for their histone binding preferences using reader domain microarrays. A subset (31) of these domains showed strong preference for the H3 N-terminal tail either unmodified or methylated at H3K4. These H3 readers were further characterized by histone peptide microarrays and/or AlphaScreen to comprehensively define their H3 preferences and PTM cross-talk.
conclusionsThe high-throughput approaches utilized in this study establish a compendium of binding information for the PHD reader family with regard to how they engage histone PTMs and uncover several novel reader domain-histone PTM interactions (i.e., PHRF1 and TRIM66). This study highlights the usefulness of high-throughput analyses of histone reader proteins as a means of understanding how chromatin engagement occurs biochemically.
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