2026-08-29T09:25:05Zhttps://repisalud.isciii.es/rest/oai/requestoai:repisalud.isciii.es:20.500.12105/74852025-03-24T15:40:51Zcom_20.500.12105_2173com_20.500.12105_2051col_20.500.12105_19597
Repisalud
author
Urdinguio, Rocio G
author
Lopez, Virginia
author
Bayón, Gustavo F
author
Diaz de la Guardia, Rafael
author
Sierra, Marta I
author
García-Toraño, Estela
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Perez, Raúl F
author
García, María G
author
Carella, Antonella
author
Pruneda, Patricia C
author
Prieto, Cristina
author
Dmitrijeva, Marija
author
Santamarina, Pablo
author
Belmonte, Thalia
author
Mangas, Cristina
author
Diaconu, Elena
author
Ferrero, Cecilia
author
Tejedor, Juan Ramón
author
Fernandez-Morera, Juan Luis
author
Bravo, Cristina
author
Bueno, Clara
author
Sanjuan-Pla, Alejandra
author
Rodriguez, Ramon M
author
Suarez-Alvarez, Beatriz
author
López-Larrea, Carlos
author
Bernal, Teresa
author
Colado, Enrique
author
Balbín, Milagros
author
García-Suarez, Olivia
author
Chiara, María Dolores
author
Sáenz-de-Santa-María, Inés
author
Rodríguez, Francisco
author
Pando-Sandoval, Ana
author
Rodrigo, Luis
author
Santos, Laura
author
Salas, Ana
author
Vallejo-Díaz, Jesús
author
C Carrera, Ana
author
Rico, Daniel
author
Hernández-López, Inmaculada
author
Vayá, Amparo
author
Ricart, José M
author
Seto, Edward
author
Sima-Teruel, Núria
author
Vaquero, Alejandro
author
Valledor, Luis
author
Cañal, Maria Jesus
author
Pisano, David
author
Graña Castro, Osvaldo
author
Thomas, Tim
author
Voss, Anne K
author
Menéndez, Pablo
author
Villar-Garea, Ana
author
Deutzmann, Rainer
author
Fernandez, Agustín F
author
Fraga, Mario F
funder
Unión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF)
funder
Gobierno del Principado de Asturias (España)
funder
Ministerio de Ciencia e Innovación (España)
funder
Instituto de Salud Carlos III
funder
Obra Social Liberbank-Cajastur (España)
2019-04-23T11:43:31Z
2019-04-23T11:43:31Z
2019-03-29
Nucleic Acids Res. 2019. pii: gkz195.
10.1093/nar/gkz195
1362-4962
0305-1048
Nucleic acids research
30923829
http://hdl.handle.net/20.500.12105/7485
Histone H4 acetylation at Lysine 16 (H4K16ac) is a key epigenetic mark involved in gene regulation, DNA repair and chromatin remodeling, and though it is known to be essential for embryonic development, its role during adult life is still poorly understood. Here we show that this lysine is massively hyperacetylated in peripheral neutrophils. Genome-wide mapping of H4K16ac in terminally differentiated blood cells, along with functional experiments, supported a role for this histone post-translational modification in the regulation of cell differentiation and apoptosis in the hematopoietic system. Furthermore, in neutrophils, H4K16ac was enriched at specific DNA repeats. These DNA regions presented an accessible chromatin conformation and were associated with the cleavage sites that generate the 50 kb DNA fragments during the first stages of programmed cell death. Our results thus suggest that H4K16ac plays a dual role in myeloid cells as it not only regulates differentiation and apoptosis, but it also exhibits a non-canonical structural role in poising chromatin for cleavage at an early stage of neutrophil cell death.
eng
Chromatin regulation by Histone H4 acetylation at Lysine 16 during cell death and differentiation in the myeloid compartment
journal article
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