ArticleNucleic acids research2014
The double PHD finger domain of MOZ/MYST3 induces α-helical structure of the histone H3 tail to facilitate acetylation and methylation sampling and modification.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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54 citing papers in PubMed, 98 citations in OpenAlex.
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- Acetyl-carnitine improves hyperactivity and learning deficits inLife science alliance · 2026Article
- Processes and therapeutic perspectives of acylation modifications of lysine and cysteine in tumors.Cell communication and signaling : CCS · 2026Review
- Lysine Acetyltransferase 6 in Health and Disease.MedComm · 2025Review
- Rare Genetic and Uncommon Morphological Entities in Adults with Acute Myeloid Leukemia.Current oncology reports · 2025Review
- Comprehensive review and outline of genotypes and phenotypes of Arboleda-Tham syndrome spectrum: insights from novel variants.Molecular biology reports · 2025Review
- Uncoupling histone modification crosstalk by engineering lysine demethylase LSD1.Nature chemical biology · 2025Article
- H3K14: A histone site closely related to diseases.Journal of Cancer · 2025Review
- Discovery and Characterization of BAY-184: A New Potent and Selective Acylsulfonamide-BenzofuranJournal of medicinal chemistry · 2024Article
- Epigenetic modulators provide a path to understanding disease and therapeutic opportunity.Genes & development · 2024Review
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- Rare Hematologic Malignancies and Pre-Leukemic Entities in Children and Adolescents Young Adults.Cancers · 2024Review
- Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024Article
- KAT6A mutations in Arboleda-Tham syndrome drive epigenetic regulation of posterior HOXC cluster.Human genetics · 2023Article
- New twists of a TAIL: novel insights into the histone binding properties of a highly conserved PHD finger cluster within the MLR family of H3K4 mono-methyltransferases.Nucleic acids research · 2023Article
- Recognition of Histone H3 Methylation States by the PHD1 Domain of Histone Demethylase KDM5A.ACS chemical biology · 2023Article
- Construction of Histone-Protein Complex Structures by Peptide Growing.International journal of molecular sciences · 2023Article
- Expression profiles and functional prediction of histone acetyltransferases of the MYST family in kidney renal clear cell carcinoma.BMC cancer · 2023Article
- The histone acetyltransferase KAT6A is recruited to unmethylated CpG islands via a DNA binding winged helix domain.Nucleic acids research · 2023Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Histone tail modifications control many nuclear processes by dictating the dynamic exchange of regulatory proteins on chromatin. Here we report novel insights into histone H3 tail structure in complex with the double PHD finger (DPF) of the lysine acetyltransferase MOZ/MYST3/KAT6A. In addition to sampling H3 and H4 modification status, we show that the DPF cooperates with the MYST domain to promote H3K9 and H3K14 acetylation, although not if H3K4 is trimethylated. Four crystal structures of an extended DPF alone and in complex with unmodified or acetylated forms of the H3 tail reveal the molecular basis of crosstalk between H3K4me3 and H3K14ac. We show for the first time that MOZ DPF induces α-helical conformation of H3K4-T11, revealing a unique mode of H3 recognition. The helical structure facilitates sampling of H3K4 methylation status, and proffers H3K9 and other residues for modification. Additionally, we show that a conserved double glycine hinge flanking the H3 tail helix is required for a conformational change enabling docking of H3K14ac with the DPF. In summary, our data provide the first observations of extensive helical structure in a histone tail, revealing the inherent ability of the H3 tail to adopt alternate conformations in complex with chromatin regulators.
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