Loss of nuclear flavanols during drought periods in Taxus baccata

Authors

  • W. Feucht,

    1.  Department for Plant Science, Unit Fruit Science, Technische Universität München, Center of Life and Food Science Weihenstephan, Freising, Germany
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  • D. Treutter,

    1.  Department for Plant Science, Unit Fruit Science, Technische Universität München, Center of Life and Food Science Weihenstephan, Freising, Germany
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  • H. Dithmar,

    1.  Department for Physical Biochemistry, Technische Universität München, Center of Life and Food Science Weihenstephan, Freising, Germany
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  • J. Polster

    1.  Department for Physical Biochemistry, Technische Universität München, Center of Life and Food Science Weihenstephan, Freising, Germany
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  • Editor
    B. Piechulla

D. Treutter, Unit Fruit Science, Department Plant Science, Duernast 2, D- 85354 Freising, Germany.
E-mail: dieter.treutter@wzw.tum.de

Abstract

Normally, needles of Taxus baccata during the growth period prominently stain blue for nuclear flavanols with the histochemical DMACA procedure. However, under excess heat and drought conditions, nuclear flavanols of current-year needles decline to zero. Nevertheless, greenish-yellow-coloured flavonols (quercetin derivatives) were still observed in nuclei. All of these yellow nuclei were in a silenced state and without mitosis. This link between drought and loss of nuclear flavanols was found in 3 years, 2003, 2007 and 2010. In 2007, exceptional drought occurred in early spring, interrupted by short rains. This, in turn, led to flushing of new sprouts, a characteristic feature in which nuclei were overloaded with flavanols. By the end of three drought periods, all nuclei developed blue-coloured nuclear flavanols. The flavanols seem to be associated with the histone proteins of chromatin. The oxidative degradation of catechin in Tris buffer (pH 8.0) containing MgCl2 was studied in the presence of the H4-core fragment TYTEHAKRKTVTAMD, modified according to the epigenetic histone code. The results show that catechin degradation can be significantly inhibited by the non-modified peptides and the methylated peptides (methylation at both lysine residues). The acetylated and formylated peptides do not show this behaviour. These observations indicate that flavanol association at chromosomes appears to be regulated by the epigenetic histone code.

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