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Mono(ADP-Ribosyl) Histone H1 in Alkylated Hepatoma Cells: Unusual Acceptor Site

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ADP-Ribosylation of Proteins

Part of the book series: Proceedings in Life Sciences ((LIFE SCIENCES))

Abstract

Treatment of cells with DNA-damaging agents like UV irradiation or alkylating chemicals is known to greatly stimulate mono- and poly(ADPR) formation [1, 2] and turnover [3, 4]. Although there are many attempts to elucidate the function of poly(ADP-ribosyl)ation in DNA repair, the role of cellular mono(ADP-ribosyl)ation in the course of DNA damage has received relatively little attention. Recently Kreimeyer et al. [5] were able to demonstrate that histones were extensively mono(ADP-ribosyl)ated in intact DMS-treated hepatoma AH7974 cells. 20–30% of DMS-induced mono(ADPR) was found to be associated with histone H1 and nearly 60% with core histones. Adamietz et al. [6] identified histone H2B as the main acceptor of mono(ADPR) under these conditions. Surprisingly, mono(ADPR)-Hl as well as mono(ADPR)-H2B conjugates seemed to be resistant towards neutral hydroxylamine, indicating a linkage between ADPR and histone that was different from the ester glycosidic bond observed with poly(ADPR) in liver nuclei [5].

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References

  1. Juarez-Salinas H, Sims HL, Jacobson MK (1979) Poly(ADP-ribose) levels in carcinogen-treated cells. Nature (London) 282:740

    Article  CAS  Google Scholar 

  2. Wielckens K, George E, Pless T, Hilz H (1983) Stimulation of poly(ADP-ribosyl)ation during Ehrlich ascites tumor cell “starvation” and suppression of concomitant DNA fragmentation by benzamide. J Biol Chem 285:4098–4104

    Google Scholar 

  3. Wielckens K, Schmidt A, George E, Bredehorst R, Hilz H (1982) DNA fragmentation and NAD depletion. J Biol Chem 257:12872–12877

    PubMed  CAS  Google Scholar 

  4. Jacobson EL, Antol KM, Juarez-Salinas H, Jacobson MK (1983) Poly(ADP-ribose) metabolism in ultraviolet irradiated human fibroblasts. J Biol Chem 258:103–107

    PubMed  CAS  Google Scholar 

  5. Kreimeyer A, Wielckens K, Adamietz P, Hilz H (1984) DNA repair-associated ADP-ribosylation in vivo. J Biol Chem 259:890–896

    PubMed  CAS  Google Scholar 

  6. Adamietz P, Rudolph A (1984) ADP-ribosylation of nuclear proteins in vivo. J Biol Chem 259: 6841–6846

    PubMed  CAS  Google Scholar 

  7. Kun E, Chang ACY, Sharma ML, Ferro AM, Nitecki D (1976) Covalent modification of proteins by metabolites of NAD+. Proc Natl Acad Sci USA 73:3131–3135

    Article  PubMed  CAS  Google Scholar 

  8. Hilz H, Koch R, Fanick W, Klapproth K, Adamietz P (1984) Nonenzymic ADP-ribosylation of specific mitochondrial polypeptides. Proc Natl Acad Sci USA 3929–3933

    Google Scholar 

  9. Hartman PG, Chapman GE, Moss T, Bradbury EM (1977) Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. Eur J Biochem 77:45–51

    Article  PubMed  CAS  Google Scholar 

  10. Allan J, Hartman PG, Crane-Robinson C, Aviles FX (1980) The structure of histone H1 and its location in chromatin. Nature (London) 288:675

    Article  CAS  Google Scholar 

  11. Böhm L, Crane-Robinson C (1984) Proteases as structural probes for chromatin: the domain structure of histones. Biosci Rep 4:365–386

    Article  PubMed  Google Scholar 

  12. Riquelme PT, Burzio LO, Koide SS (1979) ADP ribosylation of rat liver lysine-rich histone in vitro. J Biol Chem 254:3018–3928

    PubMed  CAS  Google Scholar 

  13. Ogata N, Ueda K, Kagamiyama H, Hayaishi O (1980) ADP-ribosylation of histone H1. J Biol Chem 255:7616–7620

    PubMed  CAS  Google Scholar 

  14. Braeuer HC, Adamietz P, Nellessen U, Hilz H (1981) ADP-ribosylated histone HI. Eur J Biochem 114:63–68

    Article  PubMed  CAS  Google Scholar 

  15. Sherod D, Johnson G, Chalkley R (1974) Studies on the heterogeneity of lysine-rich histones in dividing cells. J Biol Chem 249:3923–3931

    PubMed  CAS  Google Scholar 

  16. Kreimeyer A, Adamietz P, Hilz H (1985) Alkylatión-induced mono(ADP-ribosyl) histones H1 and H2B. Biol Chem Hoppe-Seyl 366:537–554

    Article  CAS  Google Scholar 

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Authors and Affiliations

  1. Institut für Physiologische Chemie der Universität Hamburg, Martinistr. 52, 2000, Hamburg 20, Germany

    Helmuth Hilz

Authors
  1. Andreas Kreimeyer
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  2. Helmuth Hilz
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Editor information

Editors and Affiliations

  1. Institut für Pharmakologie und Biochemie, Veterinärmedizinische Fakultät der Universität, CH-8057, Zürich, Switzerland

    Felix R. Althaus

  2. Physiologisch-chemisches Institut, Universität Hamburg, 2000, Hamburg 20-40, Germany

    Helmuth Hilz

  3. The University of Sussex, Biology Building, Brighton, Sussex, BN1 9QG, England

    Sydney Shall

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© 1985 Springer-Verlag Berlin Heidelberg

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Kreimeyer, A., Hilz, H. (1985). Mono(ADP-Ribosyl) Histone H1 in Alkylated Hepatoma Cells: Unusual Acceptor Site. In: Althaus, F.R., Hilz, H., Shall, S. (eds) ADP-Ribosylation of Proteins. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-70589-2_35

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  • DOI: https://doi.org/10.1007/978-3-642-70589-2_35

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-70591-5

  • Online ISBN: 978-3-642-70589-2

  • eBook Packages: Springer Book Archive

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