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Interaction of Short Peptides with FITC-Labeled Wheat Histones and Their Complexes with Deoxyribooligonucleotides

L. I. Fedoreyeva1,2, T. A. Smirnova1,2, G. Ya. Kolomijtseva2, V. Kh. Khavinson3, and B. F. Vanyushin1,2*

1All Russia Research Institute of Agricultural Biotechnology, Russian Academy of Agricultural Sciences, ul. Timiryazevskaya 42, 127550 Moscow, Russia

2Lomonosov Moscow State University, Belozersky Institute of Physico-Chemical Biology, 119991 Moscow, Russia; E-mail: vanyush@belozersky.msu.ru

3St. Petersburg Institute of Bioregulation and Gerontology, Russian Academy of Medical Sciences, pr. Dinamo 3, 197110 St. Petersburg, Russia

* To whom correspondence should be addressed.

Received July 22, 2012; Revision received October 8, 2012
Judging from fluorescence modulation (quenching), short peptides (Ala-Glu-Asp-Gly, Glu-Asp-Arg, Ala-Glu-Asp-Leu, Lys-Glu-Asp-Gly, Ala-Glu-Asp-Arg, and Lys-Glu-Asp-Trp) bind with FITC-labeled wheat histones H1, H2B, H3, and H4. This results from the interaction of the peptides with the N-terminal histone regions that contain respective and seemingly homologous peptide-binding motifs. Because homologous amino acid sequences in wheat core histones were not found, the peptides seem to bind with some core histone regions having specific conformational structure. Peptide binding with histones and histone–deoxyribooligonucleotide complexes depends on the nature of the histone and the primary structures of the peptides and oligonucleotides; thus, it is site specific. Histones H1 bind preferentially with single-stranded oligonucleotides by homologous sites in the C-terminal region of the protein. Unlike histone H1, the core histones bind predominantly with double-stranded methylated oligonucleotides and methylated DNA. Stern–Volmer constants of interaction of histone H1 and core histones with double-stranded hemimethylated oligonucleotides are higher compared with that of binding with unmethylated ones. DNA or deoxyribooligonucleotides in a complex with histones can enhance or inhibit peptide binding. It is suggested that site-specific interactions of short biologically active peptides with histone tails can serve in chromatin as control epigenetic mechanisms of regulation of gene activity and cellular differentiation.
KEY WORDS: histones, short peptides, interaction, binding, histone–oligonucleotide–peptide complexes, DNA methylation, wheat, plant, epigenetics

DOI: 10.1134/S0006297913020053