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Chromatin regulation by Histone H4 acetylation at Lysine 16 during cell death and differentiation in the myeloid compartment. 2019
Rocio G Urdinguio, and
Virginia Lopez, and
Gustavo F Bayón, and
Rafael Diaz de la Guardia, and
Marta I Sierra, and
Estela García-Toraño, and
Raúl F Perez, and
María G García, and
Antonella Carella, and
Patricia C Pruneda, and
Cristina Prieto, and
Marija Dmitrijeva, and
Pablo Santamarina, and
Thalía Belmonte, and
Cristina Mangas, and
Elena Diaconu, and
Cecilia Ferrero, and
Juan Ramón Tejedor, and
Juan Luis Fernandez-Morera, and
Cristina Bravo, and
Clara Bueno, and
Alejandra Sanjuan-Pla, and
Ramon M Rodriguez, and
Beatriz Suarez-Alvarez, and
Carlos López-Larrea, and
Teresa Bernal, and
Enrique Colado, and
Milagros Balbín, and
Olivia García-Suarez, and
María Dolores Chiara, and
Inés Sáenz-de-Santa-María, and
Francisco Rodríguez, and
Ana Pando-Sandoval, and
Luis Rodrigo, and
Laura Santos, and
Ana Salas, and
Jesús Vallejo-Díaz, and
Ana C Carrera, and
Daniel Rico, and
Inmaculada Hernández-López, and
Amparo Vayá, and
José M Ricart, and
Edward Seto, and
Núria Sima-Teruel, and
Alejandro Vaquero, and
Luis Valledor, and
Maria Jesus Cañal, and
David Pisano, and
Osvaldo Graña-Castro, and
Tim Thomas, and
Anne K Voss, and
Pablo Menéndez, and
Ana Villar-Garea, and
Rainer Deutzmann, and
Agustín F Fernandez, and
Mario F Fraga
Nanomaterials and Nanotechnology Research Center (CINN-CSIC), Universidad de Oviedo-Principado de Asturias, Spain.
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.
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