Biochemistry (Moscow)

, Volume 74, Issue 2, pp 145–152 | Cite as

H1 histone modulates DNA hydrolysis with WEN1 and WEN2 endonucleases from wheat coleoptiles

  • L. I. Fedoreyeva
  • T. A. Smirnova
  • G. Ya. Kolomijtseva
  • B. F. VanyushinEmail author


We show that total H1 histone from wheat seedlings or rat liver enhances hydrolysis of λ phage DNA with plant endonucleases WEN1 and WEN2 isolated from wheat coleoptiles. Optimal DNA/protein weight ratio in the hydrolysis reaction is 1: 1. The action of fractions I and IV (obtained from total wheat H1 histone by electrophoresis) on DNA hydrolysis with WEN1 and WEN2 enzymes depends on the DNA methylation status. Fraction IV of wheat histone H1 stimulates hydrolysis of unmethylated λ phage DNA with WEN1 and WEN2 enzymes. Hydrolysis of methylated λ phage DNA (it contains 5-methylcytosine in Cm5CWGG sequences and N6-methyladenine in Gm6ATC sites) with WEN1 is inhibited with fractions I and IV of wheat H1 histone. Fractions II and III of wheat H1 histone do not influence DNA hydrolysis with WEN1 and WEN2. S-Adenosyl-L-methionine (SAM) stimulates activity of these plant enzymes. But in the presence of H1 histone, SAM does not add to the ability of the enzyme to hydrolyze more DNA compared with that induced with H1 histone itself. Therefore, the stimulating effects of SAM and H1 histone on DNA hydrolysis with plant endonucleases may be similar. It could be suggested that SAM and H1 histone can induce more or less analogous allosteric transformations in the structure of the investigated plant endonucleases. Thus, DNA hydrolysis with plant endonucleases is modulated with total H1 histone. H1 histone fractions affect DNA hydrolysis in a different fashion; they enhance or inhibit hydrolysis depending on the DNA methylation status. We suggest that H1 histone changes site specificity of endonucleases or it might be responsible for formation of new or masking of old sites available for these enzymes due to changes in DNA structure induced in a DNA-histone complex.

Key words

apoptosis plant H1 histone endonucleases DNA methylation DNA fragmentation 



base pair


bovine serum albumin

endo G

endonuclease G




Tris-borate buffer containing EDTA


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Chikhirgina, E. V., and Vorobjev, V. I. (2002) Tsitologiya, 44, 721–735.Google Scholar
  2. 2.
    Khochbin, S. (2001) Gene, 271, 1–12.PubMedCrossRefGoogle Scholar
  3. 3.
    Lennox, R. W., Oshima, R. G., and Cohen, L. H. (1982) J. Biol. Chem., 257, 5183–5189.PubMedGoogle Scholar
  4. 4.
    Hall, J. M., and Cole, R. D. (1985) Biochemistry, 24, 7765–7771.PubMedCrossRefGoogle Scholar
  5. 5.
    Ponte, I., Vidal-Taboada, J. M., and Suau, P. (1998) Mol. Biol. Evol., 15, 702–708.PubMedGoogle Scholar
  6. 6.
    Samejima, K., Tone, S., and Earnshaw, W. C. (2001) J. Biol. Chem., 48, 45427–45432.CrossRefGoogle Scholar
  7. 7.
    Matassov, D., Kagan, T., Leblanc, J., Sikorska, M., and Zakeri, Z. (2004) Meth. Mol. Biol., 30, 1–17.Google Scholar
  8. 8.
    Liu, X., Zou, H., Widlak, P., Garrard, W., and Wang, X. (1999) J. Biol. Chem., 274, 13836–13840.PubMedCrossRefGoogle Scholar
  9. 9.
    Mizuta, R., Mizuta, M., Araki, S., Shiokawa, D., Tanuma, S., and Kitamura, D. (2006) Biochem. Biophys. Res. Commun., 345, 560–567.PubMedCrossRefGoogle Scholar
  10. 10.
    Fedoreyeva, L. I., Sobolev, D. E., and Vanyushin, B. F. (2007) Epigenetics, 2, 50–53.PubMedGoogle Scholar
  11. 11.
    Fedoreyeva, L. I., Sobolev, D. E., and Vanyushin, B. F. (2008) Biochemistry (Moscow), 73, 1000–1006.CrossRefGoogle Scholar
  12. 12.
    Smirnova, T. A., Prusov, A. N., Kolomijtseva, G. Ya., and Vanyushin, B. F. (2004) Biochemistry (Moscow), 69, 1128–1135.CrossRefGoogle Scholar
  13. 13.
    Laemmli, U. K. (1970) Nature, 227, 680–685.PubMedCrossRefGoogle Scholar
  14. 14.
    Bradford, M. M. (1976) Analyt. Biochem., 72, 248–254.PubMedCrossRefGoogle Scholar
  15. 15.
    Bakeeva, L. E., Kirnos, M. D., Aleksandrushkina, N. I., Kazimirchyuk, S. B., Shorning, B. Yu., Zamyatnina, V. A., Yaguzhinsky, L. S., and Vanyushin, B. F. (1999) FEBS Lett., 457, 122–125.PubMedCrossRefGoogle Scholar
  16. 16.
    Kodama, Y., Nagaya, S., Shinmyo, A., and Kato, K. (2007) Plant Cell Physiol., 48, 459–470.PubMedCrossRefGoogle Scholar
  17. 17.
    Gantt, J. S., and Lenvik, T. R. (1991) Eur. J. Biochem., 202, 1029–1039.PubMedCrossRefGoogle Scholar
  18. 18.
    Eden, S., and Cedar, H. (1994) Curr. Opin. Genet. Develop., 4, 255–259.CrossRefGoogle Scholar
  19. 19.
    Sternberg, N. (1985) J. Bacteriol., 164, 490–493.PubMedGoogle Scholar
  20. 20.
    Higurashi, M., and Cole, R. D. (1991) J. Biol. Chem., 266, 8619–8625.PubMedGoogle Scholar
  21. 21.
    Kas, E., Izaurralde, E., and Laemmli, U. K. (1989) J. Mol. Biol., 210, 587–599.PubMedCrossRefGoogle Scholar
  22. 22.
    McArthur, M., and Thomas, J. O. (1996) EMBO J., 15, 1705–1714.PubMedGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2009

Authors and Affiliations

  • L. I. Fedoreyeva
    • 1
    • 2
  • T. A. Smirnova
    • 1
    • 2
  • G. Ya. Kolomijtseva
    • 1
  • B. F. Vanyushin
    • 1
    • 2
    Email author
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Institute of Agricultural BiotechnologyRussian Academy of Agricultural SciencesMoscowRussia

Personalised recommendations