Number of the records: 1  

H4K5 Butyrylation Coexist with Acetylation during Human Spermiogenesis and Are Retained in the Mature Sperm Chromatin

  1. 1.
    SYSNO ASEP0563716
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleH4K5 Butyrylation Coexist with Acetylation during Human Spermiogenesis and Are Retained in the Mature Sperm Chromatin
    Author(s) de la Iglesia, O. (ES)
    Jauregi, P. (ES)
    Jodar, M. (ES)
    Barrachina, F. (ES)
    Děd, Lukáš (BTO-N) RID
    Mallofre, C. (ES)
    Rodriguez-Carunchio, L. (ES)
    Manuel Corral, J. (ES)
    Lluis Ballesca, J. (ES)
    Komrsková, Kateřina (BTO-N) ORCID
    Castillo, J. (ES)
    Oliva, R. (ES)
    Number of authors12
    Article number12398
    Source TitleInternational Journal of Molecular Sciences. - : MDPI
    Roč. 23, č. 20 (2022)
    Number of pages18 s.
    Languageeng - English
    CountryCH - Switzerland
    Keywordsbutyrylation ; acetylation ; spermatogenesis ; sperm ; sperm chromatin ; epigenetic regulation
    Subject RIVEB - Genetics ; Molecular Biology
    OECD categoryBiochemistry and molecular biology
    R&D ProjectsGJ20-17403Y GA ČR - Czech Science Foundation (CSF)
    GC20-20217J GA ČR - Czech Science Foundation (CSF)
    ED1.1.00/02.0109 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Method of publishingOpen access
    Institutional supportBTO-N - RVO:86652036
    UT WOS000875419200001
    DOI10.3390/ijms232012398
    AnnotationMale germ cells experience a drastic chromatin remodeling through the nucleo-histone to nucleo-protamine (NH-NP) transition necessary for proper sperm functionality. Post-translational modifications (PTMs) of H4 Lys5, such as acetylation (H4K5ac), play a crucial role in epigenetic control of nucleosome disassembly facilitating protamine incorporation into paternal DNA. It has been shown that butyrylation on the same residue (H4K5bu) participates in temporal regulation of NH-NP transition in mice, delaying the bromodomain testis specific protein (BRDT)-dependent nucleosome disassembly and potentially marking retained nucleosomes. However, no information was available so far on this modification in human sperm. Here, we report a dual behavior of H4K5bu and H4K5ac in human normal spermatogenesis, suggesting a specific role of H4K5bu during spermatid elongation, coexisting with H4K5ac although with different starting points. This pattern is stable under different testicular pathologies, suggesting a highly conserved function of these modifications. Despite a drastic decrease of both PTMs in condensed spermatids, they are retained in ejaculated sperm, with 30% of non-colocalizing nucleosome clusters, which could reflect differential paternal genome retention. Whereas no apparent effect of these PTMs was observed associated with sperm quality, their presence in mature sperm could entail a potential role in the zygote.
    WorkplaceInstitute of Biotechnology
    ContactMonika Kopřivová, Monika.Koprivova@ibt.cas.cz, Tel.: 325 873 700
    Year of Publishing2023
    Electronic addresshttps://www.mdpi.com/1422-0067/23/20/12398
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.