ArticleNucleic acids research2017
Molecular basis for the methylation specificity of ATXR5 for histone H3.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- Functions and Mechanisms of Histone Modifications in Plants.Annual review of plant biology · 2025Review
- A novel strategy to map a locus associated with flowering time in canola (Brassica napus L.).Molecular genetics and genomics : MGG · 2024Article
- Mitotic inheritance of genetic and epigenetic information via the histone H3.1 variant.Current opinion in plant biology · 2023Review
- Modulating epigenetic modifications for cancer therapy (Review).Oncology reports · 2023Review
- DNA polymerase epsilon binds histone H3.1-H4 and recruits MORC1 to mediate meiotic heterochromatin condensation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- H3.1K27me1 maintains transcriptional silencing and genome stability by preventing GCN5-mediated histone acetylation.The Plant cell · 2021Article
- Coupling of H3K27me3 recognition with transcriptional repression through the BAH-PHD-CPL2 complex in Arabidopsis.Nature communications · 2020Article
- Molecular recognition of nucleosomes by binding partners.Current opinion in structural biology · 2019Review
- Characteristics of a PHD Finger Subtype.Biochemistry · 2018Article
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Authors and funding
12 authors.
Funding
Abstract
In plants, the histone H3.1 lysine 27 (H3K27) mono-methyltransferases ARABIDOPSIS TRITHORAX RELATED PROTEIN 5 and 6 (ATXR5/6) regulate heterochromatic DNA replication and genome stability. Our initial studies showed that ATXR5/6 discriminate between histone H3 variants and preferentially methylate K27 on H3.1. In this study, we report three regulatory mechanisms contributing to the specificity of ATXR5/6. First, we show that ATXR5 preferentially methylates the R/F-K*-S/C-G/A-P/C motif with striking preference for hydrophobic and aromatic residues in positions flanking this core of five amino acids. Second, we demonstrate that post-transcriptional modifications of residues neighboring K27 that are typically associated with actively transcribed chromatin are detrimental to ATXR5 activity. Third, we show that ATXR5 PHD domain employs a narrow binding pocket to selectively recognize unmethylated K4 of histone H3. Finally, we demonstrate that deletion or mutation of the PHD domain reduces the catalytic efficiency (kcat/Km of AdoMet) of ATXR5 up to 58-fold, highlighting the multifunctional nature of ATXR5 PHD domain. Overall, our results suggest that several molecular determinants regulate ATXR5/6 methyltransferase activity and epigenetic inheritance of H3.1 K27me1 mark in plants.
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