Abstract 1962 Role of histone N-terminal acetylation in genome integrity
Histone modifications are key epigenetic regulators that shape chromatin structure, thereby controlling DNA accessibility for downstream processes like transcription, replication and repair. One abundant modification is histone N-terminal acetylation which is largely mediated by the N-terminal-acetyltransferase (NAT)-family member NAA40/NatD. Distinct to other NATs, NAA40 is a selective enzyme that specifically acetylates the N-alpha amino group of the first amino acid on histones H4 (Nt-acH4) and H2A (Nt-acH2A) harboring the same Ser(1)-Gly(2)-Arg(3)-Gly(4) recognition sequence.
Authors
- Till Bartke (ORCID: https://orcid.org/0000-0002-6584-2140)
- Cem Özdemir
- Till Siebenmorgen (ORCID: https://orcid.org/0009-0008-5160-8100)
- Ariel Klavaris
- Michael Sattler (ORCID: https://orcid.org/0000-0002-1594-0527)
- Antonis Kirmizis (ORCID: https://orcid.org/0000-0002-3748-8711)
- Andrey Tvardovskiy (ORCID: https://orcid.org/0000-0003-3252-280X)
- Kyle M. Miller (ORCID: https://orcid.org/0000-0002-4544-0013)
Institutions
- Cyprus University of Technology (CY)
- University of Madras (IN)
- Indian Institute of Technology Madras (IN)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109271
- Primary Topic
- Histone Deacetylase Inhibitors Research
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- Cancer Research Institute
- European Regional Development Fund