Structural organization of DNA–protein complexes of chromatin studied by vibrational and electronic circular dichroism | Zendy

A. M. Polyanichko | Zendy; H. Wieser | Zendy

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Structural organization of DNA–protein complexes of chromatin studied by vibrational and electronic circular dichroism

Author(s) -

A. M. Polyanichko,

H. Wieser

Publication year - 2010

Publication title -

spectroscopy an international journal

Language(s) - English

Resource type - Journals

eISSN - 1875-922X

pISSN - 0712-4813

DOI - 10.1155/2010/658374

Subject(s) - chromatin , circular dichroism , linker dna , chemistry , histone h1 , nucleosome , dna , high mobility group , crystallography , histone , biophysics , vibrational circular dichroism , biochemistry , biology , gene

Structure and functioning of chromatin is determined by interactions of DNA with numerous nuclear proteins. The most abundant and yet not completely understood non-histone chromosomal proteins are those belonging to a High Mobility Group (HMG) namely HMGB1. The interplay of this protein on DNA with linker histone H1 and other proteins determines both structure and functioning of the chromatin. A combination of UV and 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 (ECD) spectroscopy due to considerable light scattering in such solutions. Based on the analysis of FTIR and UV circular dichroism spectra and AFM imaging the interaction of DNA with high-mobility group non-histone chromatin protein HMGB1 and linker histone H1 was studied.

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