ArticleEpigenetics & chromatin2017
Histone peptide microarray screen of chromo and Tudor domains defines new histone lysine methylation interactions.
Article in Epigenetics & chromatin, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 60 citations in OpenAlex.
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- Rapid Single-Pot Assembly of Modular Chromatin Proteins for Epigenetic Engineering.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Engineering human JMJD2A tudor domains for an improved understanding of histone peptide recognition.Proteins · 2023Article
- De novo methylation of histone H3K23 by the methyltransferases EHMT1/GLP and EHMT2/G9a.Epigenetics & chromatin · 2022Article
- Uncovering post-translational modification-associated protein-protein interactions.Current opinion in structural biology · 2022Review
- Modified Histone Peptides Linked to Magnetic Beads Reduce Binding Specificity.International journal of molecular sciences · 2022Article
- Profiling and Validation of Live-Cell Protein Methylation with Engineered Enzymes and Methionine Analogues.Current protocols · 2021Article
- Exploring aromatic cage flexibility of the histone methyllysine reader protein Spindlin1 and its impact on binding mode prediction: an in silico study.Journal of computer-aided molecular design · 2021Article
- Structure-Based Design, Docking and Binding Free Energy Calculations of A366 Derivatives as Spindlin1 Inhibitors.International journal of molecular sciences · 2021Article
- DNMT1 reads heterochromatic H4K20me3 to reinforce LINE-1 DNA methylation.Nature communications · 2021Article
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
Abstract
backgroundHistone posttranslational modifications (PTMs) function to regulate chromatin structure and function in part through the recruitment of effector proteins that harbor specialized "reader" domains. Despite efforts to elucidate reader domain-PTM interactions, the influence of neighboring PTMs and the target specificity of many reader domains is still unclear. The aim of this study was to use a high-throughput histone peptide microarray platform to interrogate 83 known and putative histone reader domains from the chromo and Tudor domain families to identify their interactions and characterize the influence of neighboring PTMs on these interactions.
resultsNearly a quarter of the chromo and Tudor domains screened showed interactions with histone PTMs by peptide microarray, revealing known and several novel methyllysine interactions. Specifically, we found that the CBX/HP1 chromodomains that recognize H3K9me also recognize H3K23me2/3-a poorly understood histone PTM. We also observed that, in addition to their interaction with H3K4me3, Tudor domains of the Spindlin family also recognized H4K20me3-a previously uncharacterized interaction. Several Tudor domains also showed novel interactions with H3K4me as well.
conclusionsThese results provide an important resource for the epigenetics and chromatin community on the interactions of many human chromo and Tudor domains. They also provide the basis for additional studies into the functional significance of the novel interactions that were discovered.
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