Dataset Information

Both L-lactyl and D-lactyl enantiomers modify histones in mouse testis

ABSTRACT: 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.

ORGANISM(S): Mus Musculus

SUBMITTER: Delphine Pflieger

PROVIDER: PXD070274 | panorama | Tue Jun 23 00:00:00 GMT+01:00 2026

REPOSITORIES: PanoramaPublic

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Both L-lactyl and D-lactyl enantiomers modify histones in mouse testis.

Manessier Julie J Hijazi Hassan H Vizzini Lisa L Brugière Sabine S Courçon Marie M Masselon Christophe C de la Iglesia Alberto A Cocquet Julie J Pflieger Delphine D

Molecular & cellular proteomics : MCP 20260612

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 former 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 his ...[more]

PMID: 42285509

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Project description:This model is described in the article: Kinetics of histone gene expression during early development of Xenopus laevis. Koster JG, Destrée OH and Westerhoff HV. J Theor Biol. 1988 Nov 21;135(2):139-67. PMID: 3267765 Abstract: Using literature data for transcriptional and translational rate constants, gene copy numbers, DNA concentrations, and stability constants, we have calculated the expected concentrations of histones and histone mRNA during embryogenesis of Xenopus laevis. The results led us to conclude that: (i) for X. laevis the gene copy number of the histone genes is too low to ensure the synthesis of sufficient histones during very early development, inheritance from the oocyte of either histone protein or histone mRNA (but not necessarily both) is necessary; (ii) from the known storage of histones in the oocyte and the rates of histone synthesis determined by Adamson and Woodland (1977), there would be sufficient histones to structure the newly synthesized DNA up to gastrulation but not thereafter (these empirical rates of histone synthesis may be underestimates); (iii) on the other hand, the amount of H3 mRNA recently observed during early embryogenesis (Koster, 1987, Koster et al., 1988) could direct a higher and sufficient synthesis of H3 protein, also after gastrulation. We present a quantitative model that accounts both for the observed H3 mRNA concentration as a function of time during embryogenesis and for the synthesis of sufficient histones to structure the DNA throughout early embryogenesis. The model suggests that X. laevis exhibits a major (i.e. some 14-fold) reduction in transcription of histone genes approximately 11 hours after fertilization. This reduction could be due to a decrease in the number of transcribed histone genes, a decreased rate constant of transcription with continued transcription of all the histone genes, and/or a reduction in the time during the cell cycle in which histone mRNA synthesis takes place. Alternatively, the histone mRNA stability might decrease approximately 16-fold 11 hours after fertilization. This model originates from BioModels Database: A Database of Annotated Published Models. It is copyright (c) 2005-2011 The BioModels.net Team. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information. In summary, you are entitled to use this encoded model in absolutely any manner you deem suitable, verbatim, or with modification, alone or embedded it in a larger context, redistribute it, commercially or not, in a restricted way or not.. To cite BioModels Database, please use: Li C, Donizelli M, Rodriguez N, Dharuri H, Endler L, Chelliah V, Li L, He E, Henry A, Stefan MI, Snoep JL, Hucka M, Le Novère N, Laibe C (2010) BioModels Database: An enhanced, curated and annotated resource for published quantitative kinetic models. BMC Syst Biol., 4:92.

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Dataset Information

Both L-lactyl and D-lactyl enantiomers modify histones in mouse testis

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Both L-lactyl and D-lactyl enantiomers modify histones in mouse testis.

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