Interaction between linker histone H1 and non-histone chromatin protein HMGB1

Issue title: From Molecule to Tissue: XIII European Conference on the Spectroscopy of Biological Molecules, Palermo, Italy, August 28–September 2, 2009, Part 1 of 2

Article type: Research Article

Authors: Fonin, Alexander V.^{; ;} | Stepanenko, Olga V. | Kuznetsova, Irina M. | Turoverov, Konstantin K. | Kostyleva, Elena I. | Vorobyev, Vladimir I.

Affiliations: Institute of Cytology of the Russian Academy of Sciences, St. Petersburg, Russia | St. Petersburg State Politechnical University, St. Petersburg, Russia

Note: [] Corresponding author: A.V. Fonin, Institute of Cytology of the Russian Academy of Science, Tikhoretsky av. 4, 194064 St. Petersburg, Russia. Tel.: +7812 297 19 57; Fax: +7812 297 03 41; E-mail: [email protected].

Abstract: The possibility of interaction between linker histone H1 and non-histone chromatin protein HMGB1 was studied by intrinsic UV-fluorescence, far and near-UV CD and light scattering. The obtained data allow us to assume that the increase of histone H1 content in the HMGB1 solutions in a low ionic strength is accompanied by the destruction of HMGB1 associates. The interaction between proteins causes the increase of ordered regions in the protein molecules and the minor changes in their tertiary structure.

Keywords: Non-histone chromatin protein HMGB1, linker histone H1, chromatin, protein folding, intrinsically disordered proteins, intrinsic fluorescence of proteins, circular dichroism

DOI: 10.3233/SPE-2010-0417

Journal: Spectroscopy, vol. 24, no. 1-2, pp. 165-168, 2010