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| Título: | Dynamics and dispensability of variant-specific histone H1 Lys-26/Ser-27 and Thr-165 post-translational modifications |
Autor: | Terme, Jean-Michel CSIC; Millán-Ariño, Lluis CSIC; Mayor, Regina CSIC; Luque, Neus CSIC; Izquierdo-Bouldstridge, Andrea CSIC ORCID; Bustillos, Alberto; Sampaio, Cristina; Canes, Jordi; Font, Isaura; Sima, Núria; Jordan, Albert CSIC ORCID | Palabras clave: | Post-translational modifications Linker histone Histone H1 variants |
Fecha de publicación: | 27-jun-2014 | Editor: | Elsevier | Citación: | FEBS Letters 588(14): 2353-2362 (2014) | Resumen: | In mammals, the linker histone H1, involved in DNA packaging into chromatin, is represented by a family of variants. H1 tails undergo post-translational modifications (PTMs) that can be detected by mass spectrometry. We developed antibodies to analyze several of these as yet unexplored PTMs including the combination of H1.4 K26 acetylation or trimethylation and S27 phosphorylation. H1.2-T165 phosphorylation was detected at S and G2/M phases of the cell cycle and was dispensable for chromatin binding and cell proliferation; while the H1.4-K26 residue was essential for proper cell cycle progression. We conclude that histone H1 PTMs are dynamic over the cell cycle and that the recognition of modified lysines may be affected by phosphorylation of adjacent residues. © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | Descripción: | Jean-Michel Terme et al. | Versión del editor: | http://dx.doi.org/10.1016/j.febslet.2014.05.035 | URI: | http://hdl.handle.net/10261/113934 | DOI: | 10.1016/j.febslet.2014.05.035 | Identificadores: | doi: 10.1016/j.febslet.2014.05.035 issn: 1873-3468 |
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