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.

H2AX becomes phosphorylated on serine 139, then called gamma-H2AX, as a reaction on DNA Double-strand breaks (DSB). The kinases of the PIKK-family (Ataxia telangiectasia mutated, ATR and DNA-PKcs) are responsible for this phosphorylation, especially ATM. The modification can happen accidentally during replication fork collapse or in the response on ionizing radiation but also during controlled physiological processes such as V(D)J recombination. Gamma-H2AX is a sensitive target for looking at DSBs in cells. The role of the phosphorylated form of the histone in DNA repair is under discussion but it is known that because of the modification the DNA becomes less condensed. Delivering space for the recruitment of proteins necessary during repair of DSBs.

References

* [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=gene&cmd=Retrieve&dopt=full_report&list_uids=3014 ncbi]

Further reading

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

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