Dynamics and dispensability of variant-specific histone H1 Lys-26/Ser-27 and Thr-165 post-translational modifications

Jean-Michel Terme et al.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.This work was supported by the Spanish Ministry of Science and Innovation (MICINN) and European Regional Development Fund (Grant BFU2011-23057 to A.J., and Grant BFU2008-00460 to P.S.), and by the Regional Government of Catalonia (Generalitat de Catalunya; Grant 2009-SGR-1222 to A.J.). J.-M.T. received a JAE-Doc contract from the Spanish National Research Council (CSIC)-MICINN; R.M. a TA contract from CSIC-MICINN; and L.M.-A. an FPU predoctoral fellowship from MICINNPeer Reviewe

Dynamics and dispensability of variant-specific histone H1 Lys-26/Ser-27 and Thr-165 post-translational modifications

Jean-Michel Terme et al.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.This work was supported by the Spanish Ministry of Science and Innovation (MICINN) and European Regional Development Fund (Grant BFU2011-23057 to A.J., and Grant BFU2008-00460 to P.S.), and by the Regional Government of Catalonia (Generalitat de Catalunya; Grant 2009-SGR-1222 to A.J.). J.-M.T. received a JAE-Doc contract from the Spanish National Research Council (CSIC)-MICINN; R.M. a TA contract from CSIC-MICINN; and L.M.-A. an FPU predoctoral fellowship from MICINNPeer Reviewe