PXD050981-1

PXD050981 is an original dataset announced via ProteomeXchange.

Title	Function of the histone N-terminal acetyltransferase Naa40 in DNA damage response
Description	N-alpha-acetyltransferase 40 (NAA40) catalyzes acetylation on the N-terminal tip of histones H4 (N-acH4) and H2A (N-acH2A) harboring the Ser(1)-Gly(2)-Arg(3)-Gly(4) recognition sequence. In addition to the well-known role of N-terminal acetylation in protein degradation and stability, recent studies have reported the regulatory function of NAA40 and its associated histone N-terminal acetylation in different cancer types. The H2A.X histone variant, which has a critical role in DNA damage and repair, also carries the N-terminal recognition motif ‘SGRG’ at its N-terminus and could be therefore subjected to N-terminal acetylation by NAA40 (Magin et al., 2015). Prior to DNA damage, H2A.X is continuously subjected to proteasomal degradation, whereas upon the formation of double strand breaks (DSBs) is rapidly stabilized. Once incorporated into chromatin, H2A.X is phosphorylated at serine 139 (γΗ2Α.Χ) to generate γH2A.X foci that play a key role in the amplification of the DNA damage signal and the recruitment of the DNA damage checkpoint and repair machinery (Atsumi et al., 2015). Although γΗ2Α.Χ is essential in the DNA Damage Response (DDR) process, the existence and function of other marks on histone H2A.X are largely overlooked. We hypothesize that H2A.X could be a new substrate for NAA40 and that H2A.X N-terminal acetylation (N-acH2A.X) could be involved in DDR by either influencing chromatin accessibility and the recruitment of downstream DDR factors or by serving as a degradation signal (Ac/N-degron) for this histone variant (Nguyen et al., 2018). Hence, in the current study we investigated the possible N-terminal acetylation of histone H2A.X.
HostingRepository	PRIDE
AnnounceDate	2025-07-21
AnnouncementXML	Submission_2025-07-20_16:14:10.147.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Roberta Noberini
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	monomethylated residue; N6; acetylated residue; dimethylated residue
Instrument	Q Exactive Plus

Revision	Datetime	Status	ChangeLog Entry
0	2024-03-26 06:19:17	ID requested
⏵ 1	2025-07-20 16:14:10	announced

10.1186/s13072-025-00608-3;

Klavaris A, Koufaris C, Noberini R, Kouma M, Demetriadou C, Ghiringhelli A, Dietis N, Bonaldi T, Kirmizis A, H2A.X N-terminal acetylation is a newly identified NAA40-mediated modification that is responsive to UV irradiation. Epigenetics Chromatin, 18(1):46(2025) [pubmed]

submitter keyword: histone post-translational modifications, histone N-terminal acetylation

Tiziana Bonaldi
contact affiliation	European Institute of Oncology, Milan
contact email	tiziana.bonaldi@ieo.it
lab head
Roberta Noberini
contact affiliation	Istituto Europeo di Oncologia
contact email	roberta.noberini@ieo.it
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD050981
     1. Label: PRIDE project
     2. Name: Function of the histone N-terminal acetyltransferase Naa40 in DNA damage response