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.
Highlights
It became evident that many proteins can form compact ordered structure only in contact with their partners, e.g. DNA or RNA molecules, different proteins, metal ions, etc. [13]
Non-histone chromatin protein HMGB1 and linker histone H1 belong to such protein class
This paper is devoted to the study of interaction between non-histone chromatin protein HMGB1 and linker histone H1 in the wide range of ionic strength solution and different molar ratio of proteins
Summary
It became evident that many proteins can form compact ordered structure only in contact with their partners, e.g. DNA or RNA molecules, different proteins, metal ions, etc. [13]. Non-histone chromatin protein HMGB1 and linker histone H1 belong to such protein class. Both of them are the main chromatin proteins taking part in formation of high levels of chromatin structural organization. The HMGB1 tertiary structure contains two L-shaped DNA-binding domains and C-terminal acidic tail [2,9]. It can not be excluded that HMGB1 and H1 both being the linker chromatin proteins can interact with DNA and with each other. This paper is devoted to the study of interaction between non-histone chromatin protein HMGB1 and linker histone H1 in the wide range of ionic strength solution and different molar ratio of proteins. A.V. Fonin et al / Interaction between linker histone H1 and non-histone chromatin protein HMGB1
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