The effect of manganese(II) on the structure of DNA/HMGB1/H1 complexes: Electronic and vibrational circular dichroism studies

The interactions were studied of DNA with the nonhistone chromatin protein HMGB1 and histone H1 in the presence of manganese(II) ions at different protein to DNA and manganese to DNA phosphate ratios by using absorption and optical activity spectroscopy in the electronic [ultraviolet (UV) and electr...

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Veröffentlicht in:Biopolymers 2006-10, Vol.83 (2), p.182-192
Hauptverfasser: Polyanichko, A. M., Chikhirzhina, E. V., Andrushchenko, V. V., Vorob'ev, V. I., Wieser, H.
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container_end_page 192
container_issue 2
container_start_page 182
container_title Biopolymers
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creator Polyanichko, A. M.
Chikhirzhina, E. V.
Andrushchenko, V. V.
Vorob'ev, V. I.
Wieser, H.
description The interactions were studied of DNA with the nonhistone chromatin protein HMGB1 and histone H1 in the presence of manganese(II) ions at different protein to DNA and manganese to DNA phosphate ratios by using absorption and optical activity spectroscopy in the electronic [ultraviolet (UV) and electronic circular dichroism ECD)] and vibrational [infrared (IR) and vibrational circular dichroism (VCD)] regions. In the presence of Mn2+, the protein–DNA interactions differ from those without the ions and cause prominent DNA compaction and formation of large intermolecular complexes. At the same time, the presence of HMGB1 and H1 also changed the mode of interaction of Mn2+ with DNA, which now takes place mostly in the major groove of DNA involving N7(G), whereas interactions between Mn2+ and DNA phosphate groups are weakened by histone molecules. Considerable interactions were also detected of Mn2+ ions with aspartic and glutamic amino acid residues of the proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 182–192, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
doi_str_mv 10.1002/bip.20544
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At the same time, the presence of HMGB1 and H1 also changed the mode of interaction of Mn2+ with DNA, which now takes place mostly in the major groove of DNA involving N7(G), whereas interactions between Mn2+ and DNA phosphate groups are weakened by histone molecules. Considerable interactions were also detected of Mn2+ ions with aspartic and glutamic amino acid residues of the proteins. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 182–192, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. 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subjects Animals
Cattle
Circular Dichroism
DNA - chemistry
DNA - metabolism
DNA-protein interactions
histone H1
Histones - chemistry
HMGB1
HMGB1 Protein - chemistry
HMGB1 Protein - metabolism
infrared/vibrational circular dichroism spectroscopy
infrared/vibrational circular dichroism spectroscopy, HMGB1
Manganese - chemistry
Protein Binding
Spectrophotometry, Infrared
Spectrophotometry, Ultraviolet
Thymus Gland - chemistry
title The effect of manganese(II) on the structure of DNA/HMGB1/H1 complexes: Electronic and vibrational circular dichroism studies
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