H2AFX

H2AFX is one of several genes coding for histone H2A. In humans and other eukaryotes, the DNA is wrapped around histone-groups, consisting of core histones H2A, H2B, H3 and H4. Thus, the H2AFX contributes to the histone-formation and therefore the structure of DNA.

References

ncbi

Further reading

Redon C, Pilch D, Rogakou E; et al. (2002). “Histone H2A variants H2AX and H2AZ”. Curr. Opin. Genet. Dev. 12 (2): 162–9. PMID 11893489.
Fernandez-Capetillo O, Lee A, Nussenzweig M, Nussenzweig A (2005). “H2AX: the histone guardian of the genome”. DNA Repair (Amst.). 3 (8–9): 959–67. doi:10.1016/j.dnarep.2004.03.024. PMID 15279782.
Mannironi C, Bonner WM, Hatch CL (1990). “H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3′ processing signals”. Nucleic Acids Res. 17 (22): 9113–26. PMID 2587254.
Banerjee S, Smallwood A, Hultén M (1995). “ATP-dependent reorganization of human sperm nuclear chromatin”. J. Cell. Sci. 108 ( Pt 2): 755–65. PMID 7769017.
Ivanova VS, Hatch CL, Bonner WM (1994). “Characterization of the human histone H2A.X gene. Comparison of its promoter with other H2A gene promoters”. J. Biol. Chem. 269 (39): 24189–94. PMID 7929075.
Ivanova VS, Zimonjic D, Popescu N, Bonner WM (1994). “Chromosomal localization of the human histone H2A.X gene to 11q23.2-q23.3 by fluorescence in situ hybridization”. Hum. Genet. 94 (3): 303–6. PMID 8076949.
Rogakou EP, Pilch DR, Orr AH; et al. (1998). “DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139”. J. Biol. Chem. 273 (10): 5858–68. PMID 9488723.
El Kharroubi A, Piras G, Zensen R, Martin MA (1998). “Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter”. Mol. Cell. Biol. 18 (5): 2535–44. PMID 9566873.
Rogakou EP, Boon C, Redon C, Bonner WM (1999). “Megabase chromatin domains involved in DNA double-strand breaks in vivo”. J. Cell Biol. 146 (5): 905–16. PMID 10477747.
Rogakou EP, Nieves-Neira W, Boon C; et al. (2000). “Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139”. J. Biol. Chem. 275 (13): 9390–5. PMID 10734083.
Paull TT, Rogakou EP, Yamazaki V; et al. (2001). “A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage”. Curr. Biol. 10 (15): 886–95. PMID 10959836.
Deng L, de la Fuente C, Fu P; et al. (2001). “Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones”. Virology. 277 (2): 278–95. doi:10.1006/viro.2000.0593. PMID 11080476.
Chen HT, Bhandoola A, Difilippantonio MJ; et al. (2000). “Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX”. Science. 290 (5498): 1962–5. PMID 11110662.
Chadwick BP, Willard HF (2001). “Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant”. Hum. Mol. Genet. 10 (10): 1101–13. PMID 11331621.
Burma S, Chen BP, Murphy M; et al. (2001). “ATM phosphorylates histone H2AX in response to DNA double-strand breaks”. J. Biol. Chem. 276 (45): 42462–7. doi:10.1074/jbc.C100466200. PMID 11571274.
Ward IM, Chen J (2002). “Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress”. J. Biol. Chem. 276 (51): 47759–62. doi:10.1074/jbc.C100569200. PMID 11673449.
Deng L, Wang D, de la Fuente C; et al. (2001). “Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA”. Virology. 289 (2): 312–26. doi:10.1006/viro.2001.1129. PMID 11689053.
Chen A, Kleiman FE, Manley JL; et al. (2002). “Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase”. J. Biol. Chem. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591.
Zhu H, Hunter TC, Pan S; et al. (2003). “Residue-specific mass signatures for the efficient detection of protein modifications by mass spectrometry”. Anal. Chem. 74 (7): 1687–94. PMID 12033261.

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H2AFX

References

Further reading

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