PXD070921

PXD070921 is an original dataset announced via ProteomeXchange.

Title	Both L-lactyl and D-lactyl enantiomers modify histones in mouse testis
Description	Dynamic histone post-translational modifications are crucial to precisely orchestrate gene expression programs. The recently discovered histone lysine lactylation has already been explored in various pathological contexts, but less in normal tissues. This modification exists as two enantiomers, L- and D-lactylation; the first one may more likely modify histones due to abundant L-lactate produced by glycolysis. Here we report the identification by proteomics of L- and D-lactylation on lysines of histones H3 and H4 in mouse testis. We developed a targeted proteomic analysis of histone peptides using synthetic sequences modified by L- or D-lactyl, to acquire reliable identification and quantification data. Some histone peptides bearing either enantiomer are separated by reversed-phase chromatography. Interestingly, while several lysines of H3 and H4 exhibit a balanced amount of both enantiomers, residues 18 and 79 from histone H3 (H3K18 and H3K79) appear to be significantly more D-lactylated, while H3K23 is more L-lactylated. The stoichiometry of lactylation is low over the whole sequence of H3 and H4, representing 0.01 to 0.5%, which contrasts with acetylation whose abundance substantially varies between lysines. Interestingly, lactylation is more abundant than acetylation on the C-terminal half of H3 and H4. These results suggest a mechanism producing a mixture of the two enantiomers of lactate, or of a more direct substrate for lactylation, and supporting a site-selective addition of the enantiomers.
HostingRepository	PRIDE
AnnounceDate	2026-07-01
AnnouncementXML	Submission_2026-07-01_01:15:54.970.xml
DigitalObjectIdentifier	https://doi.org/10.6019/PXD070921
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Delphine PFLIEGER
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: NEWT:10090;
ModificationList	modified L-lysine residue
Instrument	Q Exactive HF

Revision	Datetime	Status	ChangeLog Entry
0	2025-11-18 17:38:45	ID requested
⏵ 1	2026-07-01 01:15:55	announced

10.6019/PXD070921;

10.1016/J.MCPRO.2026.101601;

submitter keyword: lysine lactylation,Histones, targeted proteomics

Delphine PFLIEGER
contact affiliation	University Grenoble Alpes, CEA, INSERM, UA13 BGE, CNRS, CEA, UAR 2048, Grenoble, France
contact email	delphine.pflieger@cea.fr
lab head
Delphine PFLIEGER
contact affiliation	CNRS
contact email	delphine.pflieger@cea.fr
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD070921
     1. Label: PRIDE project
     2. Name: Both L-lactyl and D-lactyl enantiomers modify histones in mouse testis