ArticleNature communications2018
Dual recognition of H3K4me3 and H3K27me3 by a plant histone reader SHL.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed.
- Epigenetic Control of Cold Stress Tolerance in Plants: Emerging Mechanisms and Applications for Crop Improvement.International journal of molecular sciences · 2026Review
- Dynamic regulatory mechanisms of histone methylation in plant development and environmental adaptation.Horticulture research · 2026Article
- Structural landscape of H3K27me3 recognition by protein domains and their potential for inhibition.The Journal of biological chemistry · 2026Review
- Direct Readout of Multivalent Chromatin Reader-Nucleosome Interactions by Nucleosome Mass Spectrometry.ACS central science · 2026Article
- H3K4me1 directs H3K36me2 and H3K36me3 deposition in land plants.Nature communications · 2026Article
- Mutation in HER1 enhances stigma exsertion and hybrid seed production in rice.Nature communications · 2026Article
- Inverse and dynamic levels of H3K4me3 and H3K27me3 regulate mouse postnatal dental gyrus development.Cell death and differentiation · 2026Article
- Role of Histone H3 Lysine 4 Methylation in Chromatin Biology.Molecules (Basel, Switzerland) · 2025Review
- A nucleoporin-associated signaling cascade controls plant immunity via histone modification.Genome biology · 2025Article
- The Emerging Role of the Salt Tolerance-Related Protein in the Abiotic Stress Response ofPlants (Basel, Switzerland) · 2025Review
- Epigenetically poised chromatin states regulateaBIOTECH · 2025Article
- Functions and Mechanisms of Histone Modifications in Plants.Annual review of plant biology · 2025Review
- O-Fucosyltransferase SPINDLY attenuates auxin-induced fruit growth by inhibiting ARF6/8-coactivator mediator complex interaction in Arabidopsis.Nature communications · 2025Article
- The C-terminal PHDVC5HCH tandem domain of NSD2 is a combinatorial reader of unmodified H3K4 and tri-methylated H3K27 that regulates transcription of cell adhesion genes in multiple myeloma.Nucleic acids research · 2025Article
- EMBRYONIC FLOWER 1 regulates male reproduction by repressing the jasmonate pathway downstream transcription factor MYB26.The Plant cell · 2024Article
- A repressive H3K36me2 reader mediates Polycomb silencing.Nature communications · 2024Article
- Actively Expressed Intergenic Genes Generated by Transposable Element Insertions inPlants (Basel, Switzerland) · 2024Article
- Nucleosomal asymmetry: a novel mechanism to regulate nucleosome function.Biochemical Society transactions · 2024Review
- Genome-wide profiling of histone (H3) lysine 4 (K4) tri-methylation (me3) under drought, heat, and combined stresses in switchgrass.BMC genomics · 2024Article
- Temporally-coordinated bivalent histone modifications of BCG1 enable fungal invasion and immune evasion.Nature communications · 2024Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors.
Funding
Abstract
The ability of a cell to dynamically switch its chromatin between different functional states constitutes a key mechanism regulating gene expression. Histone mark "readers" display distinct binding specificity to different histone modifications and play critical roles in regulating chromatin states. Here, we show a plant-specific histone reader SHORT LIFE (SHL) capable of recognizing both H3K27me3 and H3K4me3 via its bromo-adjacent homology (BAH) and plant homeodomain (PHD) domains, respectively. Detailed biochemical and structural studies suggest a binding mechanism that is mutually exclusive for either H3K4me3 or H3K27me3. Furthermore, we show a genome-wide co-localization of SHL with H3K27me3 and H3K4me3, and that BAH-H3K27me3 and PHD-H3K4me3 interactions are important for SHL-mediated floral repression. Together, our study establishes BAH-PHD cassette as a dual histone methyl-lysine binding module that is distinct from others in recognizing both active and repressive histone marks.
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