ArticleJournal of molecular biology2017
Structural Insight into Recognition of Methylated Histone H3K4 by Set3.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed.
- Positive Regulation of Soybean Seed Vigor and Quality by the Zinc Finger Transcription Factor GmPHD3 Under High-Temperature and High-Humidity Stress.Plants (Basel, Switzerland) · 2026Article
- Bipartite chromatin recognition by Hop1 from two diverged Holozoa.Life science alliance · 2025Article
- Structural and functional analysis of the SET3 histone deacetylase complex.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Structural insight into ASH1L PHD finger recognizing methylated histone H3K4 and promoting cell growth in prostate cancer.Frontiers in oncology · 2022Article
- Searching for methyllysine-binding aromatic cages.The Biochemical journal · 2021Article
- The PHD finger of Spp1 mediates histone modification cross-talk.The Biochemical journal · 2019Article
- SET domains and stress: uncovering new functions for yeast Set4.Current genetics · 2019Review
- Set4 is a chromatin-associated protein, promotes survival during oxidative stress, and regulates stress response genes in yeast.The Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The plant homeodomain (PHD) finger of Set3 binds methylated lysine 4 of histone H3 in vitro and in vivo; however, precise selectivity of this domain has not been fully characterized. Here, we explore the determinants of methyllysine recognition by the PHD fingers of Set3 and its orthologs. We use X-ray crystallographic and spectroscopic approaches to show that the Set3 PHD finger binds di- and trimethylated states of H3K4 with comparable affinities and employs similar molecular mechanisms to form complexes with either mark. Composition of the methyllysine-binding pocket plays an essential role in determining the selectivity of the PHD fingers. The finding that the histone-binding activity is not conserved in the PHD finger of Set4 suggests different functions for the Set3 and Set4 paralogs.
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Registered trials
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