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Histone H2AX in DNA repair

Treść / Zawartość
Identyfikatory
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The paper reviews the recent reports on the role of the phosphorylated histone H2AX (gamma-H2AX). The modification of this histone is an important part of the cellular response to the induction of DNA double strand breaks (DSB) by ionising radiation and other DSB-generating factors. In irradiated cell the modification is carried out mainly by ATM (ataxia- -telangiectasia mutated) kinase, the enzyme that starts the alarm signalling upon induction of DSB. gamma-H2AX molecules are formed within 1 3 min after irradiation and form foci at the sites of DSB. This seems to be necessary for the recruitment of repair factors that are later present in foci of damaged nuclei. Modification of a constant percentage of H2AX molecules per DSB takes place, corresponding to chromatin domains of megabase pairs of DNA.
Czasopismo
Rocznik
Strony
127--131
Opis fizyczny
Bibliogr. 19 poz., rys.
Twórcy
  • Department of Radiobiology and Health Protection, Institute of Nuclear Chemistry and Technology, 16 Dorodna Str., 03-195 Warszawa, Poland Tel./Fax: +48 22/ 811 07 36
autor
  • Department of Radiobiology and Health Protection, Institute of Nuclear Chemistry and Technology, 16 Dorodna Str., 03-195 Warszawa, Poland Tel./Fax: +48 22/ 811 07 36
Bibliografia
  • 1. Andegeko Y, Moyal L, Mittelman L, Tsarfaty I, Shiloh Y, Rotman G (2001) Nuclear retention of ATM at sites of DNA double strand breaks. J Biol Chem 276:38224−38230
  • 2. Badie C, Iliakis G, Foray N et al. (1995) Induction and rejoining of DNA double-strand breaks and interphase chromosome breaks after exposure to X rays in one normal and two hypersensitive human fibroblast cell lines. Radiat Res 144:26−35
  • 3. Brownell JE, Zhou J, Ranalli T et al. (1996) Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843−851
  • 4. Burma S, Chen BP, Murphy M, Kurimasa A, Chen DJ (2001) ATM phosphorylates histone H2AX in response to DNA double-strand breaks. J Biol Chem 276:42462−42467
  • 5. Carbone R, Pearson M, Minucci S, Pelicci PG (2002) PML NBs associate with the hMre11 complex and p53 at sites of irradiation induced DNA damage. Oncogene 21:1633−1640
  • 6. Chen HT, Bhandoola A, Difilippantonio MJ et al. (2000) Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX. Science 29:1962−1965
  • 7. Costanzo V, Robertson K, Bibikova M et al. (2001) Mre11 protein complex prevents double-strand break accumulation during chromosomal DNA replication. Mol Cell 8:137−147
  • 8. Downs JA, Lowndes NF, Jackson SP (2000) A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature 408:1001−1004
  • 9. Gately DP, Hittle JC, Chan GK, Yen TJ (1998) Characterization of ATM expression, localization, and associated DNA-dependent protein kinase activity. Mol Biol Cell 9:2361−2374
  • 10. Hoppe BS, Jensen RB, Kirchgessner CU (2000) Complementation of the radiosensitive M059J cell line. Radiat Res 153:125−130
  • 11. Maser RS, Monsen KJ, Nelms BE, Petrini JH (1997) hMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks. Mol Cell Biol 17:6087−6096
  • 12. O’Neill LP, Turner BM (1995) Histone H4 acetylation distinguishes coding regions of the human genome from heterochromatin in a differentiation-dependent but transcription-independent manner. EMBO J 14:3946−3957
  • 13. Paull TT, Rogakou EP, Yamazaki V, Kirchgessner CU, Gellert M, Bonner WM (2000) A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr Biol 10:886−895
  • 14. Petersen S, Casellas R, Reina-San-Martin B et al. (2001) AID is required to initiate Nbs1/gamma-H2AX focus formation and mutations at sites of class switching. Nature 414:660−665
  • 15. Redon C, Pilch D, Rogakou E, Sedelnikova O, Newrock K, Bonner W (2002) Histone H2A variants H2AX and H2AZ. Curr Opin Genet Dev 12:162−169
  • 16. Rogakou EP, Boon C, Redon C, Bonner WM (1999) Megabase chromatindomains involved in DNA double-strand breaks in vivo. J Cell Biol 146:905−916
  • 17. Rogakou EP, Nieves-Neira W, Boon C, Pommier Y, Bonner WM (2000) Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139. J Biol Chem 275:9390−9395
  • 18. Rogakou EP, Pilch DR, Orr AH, Ivanova VS, Bonner WM (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 273:5858−5868
  • 19. Szumiel I (1998) Monitoring and signalling of radiation-induced damage in mammalian cells. Radiat Res 150;S1:s92−s101
Typ dokumentu
Bibliografia
Identyfikator YADDA
bwmeta1.element.baztech-article-BUJ6-0006-0046
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