H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin

Male 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 nucleos...

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Autores: de la Iglesia Rodriguez, Alberto, Jauregi, Paula, Jodar Bifet, Meritxell, Barrachina, Ferran, Ded, Lukas, Mallofré i Gómez, Carme, Rodríguez-Carunchio, Leonardo, Corral, Juan Manuel, Ballescà, Josep Lluís, Komrskova, Katerina, Castillo Corullón, Judit, Oliva Virgili, Rafael
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/190353
Acceso en línea:https://hdl.handle.net/2445/190353
Access Level:acceso abierto
Palabra clave:Espermatozoides
Espermatogènesi
Cromatina
Spermatozoa
Spermatogenesis
Chromatin
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spelling H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatinde la Iglesia Rodriguez, AlbertoJauregi, PaulaJodar Bifet, MeritxellBarrachina, FerranDed, LukasMallofré i Gómez, CarmeRodríguez-Carunchio, LeonardoCorral, Juan ManuelBallescà, Josep LluísKomrskova, KaterinaCastillo Corullón, JuditOliva Virgili, RafaelEspermatozoidesEspermatogènesiCromatinaSpermatozoaSpermatogenesisChromatinMale 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.MDPI2022info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/190353Articles publicats en revistes (Biomedicina)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.3390/ijms232012398International Journal of Molecular Sciences, 2022, vol. 23, num. 20 (12398), p. 1-18https://doi.org/10.3390/ijms232012398cc-by (c) de la Iglesia Rodriguez, Alberto et al., 2022https://creativecommons.org/licenses/by/4.0/info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1903532026-05-27T06:46:51Z
dc.title.none.fl_str_mv H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
title H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
spellingShingle H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
de la Iglesia Rodriguez, Alberto
Espermatozoides
Espermatogènesi
Cromatina
Spermatozoa
Spermatogenesis
Chromatin
title_short H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
title_full H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
title_fullStr H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
title_full_unstemmed H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
title_sort H4K5 butyrylation coexist with acetylation during human spermiogenesis and are retained in the mature sperm chromatin
dc.creator.none.fl_str_mv de la Iglesia Rodriguez, Alberto
Jauregi, Paula
Jodar Bifet, Meritxell
Barrachina, Ferran
Ded, Lukas
Mallofré i Gómez, Carme
Rodríguez-Carunchio, Leonardo
Corral, Juan Manuel
Ballescà, Josep Lluís
Komrskova, Katerina
Castillo Corullón, Judit
Oliva Virgili, Rafael
author de la Iglesia Rodriguez, Alberto
author_facet de la Iglesia Rodriguez, Alberto
Jauregi, Paula
Jodar Bifet, Meritxell
Barrachina, Ferran
Ded, Lukas
Mallofré i Gómez, Carme
Rodríguez-Carunchio, Leonardo
Corral, Juan Manuel
Ballescà, Josep Lluís
Komrskova, Katerina
Castillo Corullón, Judit
Oliva Virgili, Rafael
author_role author
author2 Jauregi, Paula
Jodar Bifet, Meritxell
Barrachina, Ferran
Ded, Lukas
Mallofré i Gómez, Carme
Rodríguez-Carunchio, Leonardo
Corral, Juan Manuel
Ballescà, Josep Lluís
Komrskova, Katerina
Castillo Corullón, Judit
Oliva Virgili, Rafael
author2_role author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Espermatozoides
Espermatogènesi
Cromatina
Spermatozoa
Spermatogenesis
Chromatin
topic Espermatozoides
Espermatogènesi
Cromatina
Spermatozoa
Spermatogenesis
Chromatin
description Male 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.
publishDate 2022
dc.date.none.fl_str_mv 2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/190353
url https://hdl.handle.net/2445/190353
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Reproducció del document publicat a: https://doi.org/10.3390/ijms232012398
International Journal of Molecular Sciences, 2022, vol. 23, num. 20 (12398), p. 1-18
https://doi.org/10.3390/ijms232012398
dc.rights.none.fl_str_mv cc-by (c) de la Iglesia Rodriguez, Alberto et al., 2022
https://creativecommons.org/licenses/by/4.0/
info:eu-repo/semantics/openAccess
rights_invalid_str_mv cc-by (c) de la Iglesia Rodriguez, Alberto et al., 2022
https://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv Articles publicats en revistes (Biomedicina)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301603

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