ArticleNature chemical biology2019
DNA repair complex licenses acetylation of H2A.Z.1 by KAT2A during transcription.
Article in Nature chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- RUNX1 recruitment of GCN5 in keratinocytes upregulates ICOSLG and promotes T cell activation in the psoriasis microenvironment.Experimental & molecular medicine · 2026Article
- Identification of the regulatory elements and protein substrates of lysine acetoacetylation.eLife · 2026Article
- Identification of post-translational modification-related biomarkers in ischemic stroke using bioinformatics and machine learning.Scientific reports · 2025Article
- Identification of the Regulatory Elements and Protein Substrates of Lysine Acetoacetylation.bioRxiv : the preprint server for biology · 2025Article
- H2A.Z is essential for oocyte maturation and fertility in female mouse.Nature structural & molecular biology · 2025Article
- High Sugar Induced RCC2 Lactylation Drives Breast Cancer Tumorigenicity Through Upregulating MAD2L1.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The "Ins and Outs and What-Abouts" of H2A.Z: A tribute to C. David Allis.The Journal of biological chemistry · 2025Article
- The advances in acetylation modification in senescence and aging-related diseases.Frontiers in physiology · 2025Review
- The Dynamics of Histone Modifications during Mammalian Zygotic Genome Activation.International journal of molecular sciences · 2024Review
- MicroRNA-455-3p accelerate malignant progression of tumor by targeting H2AFZ in colorectal cancer.Cell cycle (Georgetown, Tex.) · 2023Article
- Integrative analysis of histone acetyltransferase KAT2A in human cancer.Cancer biomarkers : section A of Disease markers · 2023Article
- Tip60-mediated H2A.Z acetylation promotes neuronal fate specification and bivalent gene activation.Molecular cell · 2022Article
- GCN5-mediated regulation of pathological cardiac hypertrophy via activation of the TAK1-JNK/p38 signaling pathway.Cell death & disease · 2022Article
- TmcA functions as a lysine 2-hydroxyisobutyryltransferase to regulate transcription.Nature chemical biology · 2022Article
- DNA Damage Repair-Related Genes Signature for Immune Infiltration and Outcome in Cervical Cancer.Frontiers in genetics · 2022Article
- Structure of HIV-1 Vpr in complex with the human nucleotide excision repair protein hHR23A.Nature communications · 2021Article
- Schizosaccharomyces pombe KAT5 contributes to resection and repair of a DNA double-strand break.Genetics · 2021Article
- The bromodomains of BET family proteins can recognize diacetylated histone H2A.Z.Protein science : a publication of the Protein Society · 2021Article
- The E2F1 transcription factor and RB tumor suppressor moonlight as DNA repair factors.Cell cycle (Georgetown, Tex.) · 2020Review
- The roles of histone variants in fine-tuning chromatin organization and function.Nature reviews. Molecular cell biology · 2020Review
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Post-translational modifications of histone variant H2A.Z accompany gene transactivation, but its modifying enzymes still remain elusive. Here, we reveal a hitherto unknown function of human KAT2A (GCN5) as a histone acetyltransferase (HAT) of H2A.Z at the promoters of a set of transactivated genes. Expression of these genes also depends on the DNA repair complex XPC-RAD23-CEN2. We established that XPC-RAD23-CEN2 interacts both with H2A.Z and KAT2A to drive the recruitment of the HAT at promoters and license H2A.Z acetylation. KAT2A selectively acetylates H2A.Z.1 versus H2A.Z.2 in vitro on several well-defined lysines and we unveiled that alanine-14 in H2A.Z.2 is responsible for inhibiting the activity of KAT2A. Notably, the use of a nonacetylable H2A.Z.1 mutant shows that H2A.Z.1ac recruits the epigenetic reader BRD2 to promote RNA polymerase II recruitment. Our studies identify KAT2A as an H2A.Z.1 HAT in mammals and implicate XPC-RAD23-CEN2 as a transcriptional co-activator licensing the reshaping of the promoter epigenetic landscape.
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