The HMG1 Ta(i)le

Polyanichko, A. M.; Чихиржина, Е. В.; Skvortsov, A. N.; Kostyleva, E. I.; Colson, Pierre; Houssier, Claude; Воробьев, В. И.

doi:10.1080/07391102.2002.10506808

Cited by 32 publications

(19 citation statements)

References 25 publications

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“…The HMGB1 protein showed cooperativity in HMGB1-DNA binding. It was previously shown that increase in the concentration of HMGB1 in the system facilitates DNA binding and results in the formation of ordered supramolecular complexes (Polianichko et al, 2002(Polianichko et al, , 2013. The formation of these supramolecular complexes also explains the observed difference in complex mobility with increase in protein concentrations.…”

Section: Discussionmentioning

confidence: 59%

Ability of HMGB1 protein to bind to intrinsically bent and non-bent DNA sites in the AMPD2 gene amplicon

et al. 2016

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ABSTRACT. HMGB-like proteins are architectural chromatin factors, and their function is heavily dependent on their ability to interact with DNA (especially non-canonical DNA structures). HMGB1 is involved in many DNA processes, and dysregulation of HMGB protein expression has profound effects on cellular transcription, resulting in severe developmental defects as well as cancer. During DNA replication, elements that form the origin are still not well defined in metazoans. Sites with A (adenine) or T (thymine) repeats cause intrinsic curvatures in the DNA and are described to be involved in the replication machinery by providing binding sites to replication proteins. As a result, the DNA molecule shows intrinsically bent DNA sites, caused by periodic repeats of 2 or more As/Ts (dA/dT) as well as intrinsically non-bent DNA sites (INBDs), due to a succession of curvatures that cancel each other. In the present study, we mapped 11 INBDSs present in the AMPD2 gene that are related to each replication origin (oriGNAI3, oriC, oriB, and oriA). Following characterization of INBDSs, we tested the ability of HMGB1 to bind to the bent (b1, b2, b4a, b4b, b5, b6, b7, and b8) and non-bent DNA fragments (nb7, nb11, nb1, nb2, nb4, and nb5) via electrophoretic mobility shift assays. All fragments showed efficient binding to HMGB1. However, the non-bent DNA fragments nb2, nb4, and nb5 showed slightly reduced binding efficiency.

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Section: Discussionmentioning

confidence: 59%

Ability of HMGB1 protein to bind to intrinsically bent and non-bent DNA sites in the AMPD2 gene amplicon

et al. 2016

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“…The spectral behavior of the complexes in the UV region is different for the Mn 2þ -DNA-protein complex than for the DNA-protein 36,43,68,69 and Mn 2þ -DNA 52 complexes and depends on the protein to DNA ratio. The ECD spectra of the complexes indicate that several structural stages are occurring in the system, depending on the protein to DNA ratio (Figure 3), and supramolecular structures are formed during these stages.…”

Section: Discussionmentioning

confidence: 96%

“…18,23,[26][27][28][29][30][31][32][33] Protein-protein interactions affect many DNA binding properties of HMGB1, especially in complex DNA-protein systems. [34][35][36] It was shown recently that HMGB proteins modulate some recombination events. [13][14][15][16] Histone H1 is one of the most studied chromatin proteins.…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2006

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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.

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“…10,13,18,[20][21][22] Protein-protein interactions affect strongly DNA-binding properties of HMGB1 especially in complex DNA-protein systems. [23][24][25] Histone H1 is one of the best studied chromatin proteins. [26][27][28][29] It binds to linker DNA at the entrance or exit of the nucleosome.…”

Section: Introductionmentioning

confidence: 99%

Fourier transform infrared/vibrational circular dichroism spectroscopy as an informative tool for the investigation of large supramolecular complexes of biological macromolecules

Polyanichko

Wieser

2005

Biopolymers

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A combination of ultraviolet (UV) and infrared (IR) absorption and circular dichroism (CD) spectroscopy was applied to investigate the structure and formation of large supramolecular DNA-protein complexes. This combination of techniques was used to overcome limitations of UV-CD (electronic, or ECD) spectroscopy due to considerable light scattering in such solutions. Based on the analysis of FTIR and UV-CD spectra, the interaction of DNA with nonhistone chromatin protein HMGB1 and linker histone H1 was studied. The data obtained showed that under the conditions of the experiment (15 mM NaCl, protein/DNA ratio r < 1 w/w) the proteins did not reveal any AT or GC specificity in binding to DNA. In the presence of both proteins, mainly interactions in the DNA minor groove were observed, which were attributed to HMGB1 binding. Histone H1 facilitated binding of HMGB1 to DNA by interacting with the negatively charged groups of the sugar-phosphate backbone and binding of aspartic and glutamic amino acid residues of HMGB1. Acting together, HMGB1 and H1 stimulated the assemblage of supramolecular DNA-protein structures. The structural organization of the ternary complexes depended not only on the properties of the protein-DNA interactions but also on the interactions between HMGB1 and H1 molecules.

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The HMG1 Ta(i)le

Cited by 32 publications

References 25 publications

Ability of HMGB1 protein to bind to intrinsically bent and non-bent DNA sites in the AMPD2 gene amplicon

Ability of HMGB1 protein to bind to intrinsically bent and non-bent DNA sites in the AMPD2 gene amplicon

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

Fourier transform infrared/vibrational circular dichroism spectroscopy as an informative tool for the investigation of large supramolecular complexes of biological macromolecules

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