L’acétylation des histones - Un nouveau maillon de la chaîne d’assemblage du nucléosome

Hugo Wurtele; Qin Li; Hui Zhou; Zhiguo Zhang; Alain Verreault

doi:10.1051/medsci/2009252121

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Volume 25 / Numéro 2 (Février 2009)

Med Sci (Paris), 25 2 (2009) 121-122

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Numéro		Med Sci (Paris) Volume 25, Numéro 2, Février 2009


Page(s)		121 - 122
Section		Nouvelles
DOI		https://doi.org/10.1051/medsci/2009252121
Publié en ligne		15 février 2009

Bertin A, Mangenot S. Structure et dynamique de la particule cœur de nucléosome. Med Sci (Paris) 2008; 24 : 715–9. [Google Scholar]
Li Q, Zhou H, Wurtele H, et al. Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 2008; 134 : 244–55. [Google Scholar]
Verreault A, Kaufman PD, Kobayashi, R, et al. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 1996; 87 : 95–104. [Google Scholar]
Zhou H, Madden BJ, Muddiman DC, et al. Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair. Biochemistry 2006; 45 : 2852–61. [Google Scholar]
Ma XJ, Wu, J, Altheim, BA, et al. Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast. Proc Natl Acad Sci USA 1998; 95 : 6693–8. [Google Scholar]
Blackwell JS Jr, Wilkinson ST, Mosammaparast N, et al. Mutational analysis of H3 and H4 N termini reveals distinct roles in nuclear import. J Biol Chem 2007; 282 : 20142–50. [Google Scholar]
Masumoto H, Hawke D, Kobayashi R, et al. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005; 436 : 294–8. [Google Scholar]
Xhemalce B, Miller KM, Driscoll R, et al. Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe. J Biol Chem 2007; 282 : 15040–7. [Google Scholar]
Chen CC, Carson JJ, Feser J, et al. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 2008; 134 : 231–43. [Google Scholar]
Maas NL, Miller KM, DeFazio LG, et al. Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol Cell 2006; 23 : 109–19. [Google Scholar]
Garcia BA, Hake SB, Diaz RL, et al. Organismal differences in post-translational modifications in histones H3 and H4. J Biol Chem 2007; 282 : 7641–55. [Google Scholar]

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[1] Bertin A, Mangenot S. Structure et dynamique de la particule cœur de nucléosome. Med Sci (Paris) 2008; 24 : 715–9. [Google Scholar]

[2] Li Q, Zhou H, Wurtele H, et al. Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 2008; 134 : 244–55. [Google Scholar]

[3] Verreault A, Kaufman PD, Kobayashi, R, et al. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 1996; 87 : 95–104. [Google Scholar]

[4] Zhou H, Madden BJ, Muddiman DC, et al. Chromatin assembly factor 1 interacts with histone H3 methylated at lysine 79 in the processes of epigenetic silencing and DNA repair. Biochemistry 2006; 45 : 2852–61. [Google Scholar]

[5] Ma XJ, Wu, J, Altheim, BA, et al. Deposition-related sites K5/K12 in histone H4 are not required for nucleosome deposition in yeast. Proc Natl Acad Sci USA 1998; 95 : 6693–8. [Google Scholar]

[6] Blackwell JS Jr, Wilkinson ST, Mosammaparast N, et al. Mutational analysis of H3 and H4 N termini reveals distinct roles in nuclear import. J Biol Chem 2007; 282 : 20142–50. [Google Scholar]

[7] Masumoto H, Hawke D, Kobayashi R, et al. A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 2005; 436 : 294–8. [Google Scholar]

[8] Xhemalce B, Miller KM, Driscoll R, et al. Regulation of histone H3 lysine 56 acetylation in Schizosaccharomyces pombe. J Biol Chem 2007; 282 : 15040–7. [Google Scholar]

[9] Chen CC, Carson JJ, Feser J, et al. Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 2008; 134 : 231–43. [Google Scholar]

[10] Maas NL, Miller KM, DeFazio LG, et al. Cell cycle and checkpoint regulation of histone H3 K56 acetylation by Hst3 and Hst4. Mol Cell 2006; 23 : 109–19. [Google Scholar]

[11] Garcia BA, Hake SB, Diaz RL, et al. Organismal differences in post-translational modifications in histones H3 and H4. J Biol Chem 2007; 282 : 7641–55. [Google Scholar]