ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 38 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
38 citing papers in PubMed, 65 citations in OpenAlex.
- Histone acetyltransferases as integrative epigenetic regulators of plant abiotic stress responses.Plant cell reports · 2026Review
- Schistosoma japonicum histone acetyltransferase 1 (SjHAT1): A novel anti-schistosomal drug target.PLoS pathogens · 2026Article
- Inhibition of Histone Lysine Acetyltransferases by Coenzyme A Analogs.Molecules (Basel, Switzerland) · 2026Article
- The Histone Acetyltransferase CgHat1 Regulates Growth, Development, and Pathogenicity ofJournal of fungi (Basel, Switzerland) · 2025Article
- The Dual Role of RBBP7 in Esophageal Squamous Cell Carcinoma: Cell Context-Dependent Impacts on Proliferation and Radiosensitivity.OncoTargets and therapy · 2025Article
- Profiling nuclear cysteine ligandability and effects on nuclear localization using proximity labeling-coupled chemoproteomics.Cell chemical biology · 2024Article
- Acetyl-Click Screening Platform Identifies Small-Molecule Inhibitors of Histone Acetyltransferase 1 (HAT1).Journal of medicinal chemistry · 2023Article
- Understanding HAT1: A Comprehensive Review of Noncanonical Roles and Connection with Disease.Genes · 2023Review
- Review
- Identification and characterization of a novel GNAT superfamily NMicrobial biotechnology · 2022Article
- Topography of histone H3-H4 interaction with the Hat1-Hat2 acetyltransferase complex.Genes & development · 2022Article
- Histone lysine methacrylation is a dynamic post-translational modification regulated by HAT1 and SIRT2.Cell discovery · 2021Article
- Recent insights intoEpigenetics · 2021Review
- Harnessing Ionic Selectivity in Acetyltransferase Chemoproteomic Probes.ACS chemical biology · 2021Article
- Substrate Scope for Human Histone Lysine Acetyltransferase KAT8.International journal of molecular sciences · 2021Article
- Identification of lysine isobutyrylation as a new histone modification mark.Nucleic acids research · 2021Article
- Post-translational Lysine Ac(et)ylation in Bacteria: A Biochemical, Structural, and Synthetic Biological Perspective.Frontiers in microbiology · 2021Review
- Protein acetylation and deacetylation: An important regulatory modification in gene transcription (Review).Experimental and therapeutic medicine · 2020Review
- HAT1 Coordinates Histone Production and Acetylation via H4 Promoter Binding.Molecular cell · 2019Article
- Bisubstrate inhibitors to target histone acetyltransferase 1.Chemical biology & drug design · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Histone acetyltransferase 1 is the founding member of the histone acetyltransferase superfamily and catalyzes lysine acetylation of newly synthesized histone H4. Here we report a 1.9-Å resolution crystal structure of human histone acetyltransferase 1 in complex with acetyl coenzyme A and histone H4 peptide. The crystal structure reveals that the cofactor and the side chain of lysine 12 of histone H4 peptide are placed in the canyon between the central and C-terminal domains. Histone H4 peptide adopts a well-defined conformation and establishes an extensive set of interactions with the enzyme including invariant residues Glu64 and Trp199, which together govern substrate-binding specificity of histone acetyltransferase 1. Our structure-guided enzyme kinetic study further demonstrates a cumulative effect of the active-site residues Glu187, Glu276, and Asp277 on deprotonation of the ε-amino group of reactive Lys12 for direct attack of the acetyl group of the cofactor.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.