ArticleACS chemical biology2023
Effects of Oncohistone Mutations and PTM Crosstalk on the N-Terminal Acetylation Activities of NatD.
Article in ACS chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD.Science advances · 2025Article
- A Cell-Potent Bisubstrate Inhibitor to Probe NatD Acetyltransferase Activity.ACS chemical biology · 2025Article
- H2A.X N-terminal acetylation is a newly identified NAA40-mediated modification that is responsive to UV irradiation.Epigenetics & chromatin · 2025Article
- Purification and activity assays of N-terminal acetyltransferase D.Methods in enzymology · 2025Article
- De novo methylation of histone H3K23 by the methyltransferases EHMT1/GLP and EHMT2/G9a.Epigenetics & chromatin · 2022Article
- Virtual Special Issue: Epigenetics 2022.ACS pharmacology & translational science · 2022Article
- Virtual Special Issue: Epigenetics 2022.ACS medicinal chemistry letters · 2022Article
- Oncohistones: Exposing the nuances and vulnerabilities of epigenetic regulation.Molecular cell · 2022Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Acetylation at the α-N-terminus (Nα) is the most abundant modification detected on histone H4 and H2A, which is catalyzed by N-terminal acetyltransferase D (NatD or NAA40). Histone H4 and H2A contain an identical N-terminal SGRGK sequence that is enriched with post-translational modifications (PTMs) and frequently occurred oncogenic mutations known as "oncohistone" mutations. However, there is a lack of information on how oncohistone mutations and other PTMs affect NatD-catalyzed acetylation. Herein, we determined how the local chemical environment on the N-terminal SGRGK sequence impacts NatD-catalyzed Nα-acetylation on histone H4/H2A. Our studies indicate that all oncohistone mutations at SGRG suppressed NatD-catalyzed acetylation. Meanwhile, H4 Ser1 phosphorylation and Arg3 methylation negatively impact the NatD-mediated acetylation, but the Lys5 acetylation only has a marginal effect. This work reveals the impacts of oncohistone mutations on NatD activity and unravels the crosstalk between NatD and PTMs, implying potential regulatory mechanism of NatD and highlighting different avenues to interrogate the NatD-mediated pathway in the future.
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Registered trials
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