Binding of Histone H1 to DNA Is Differentially Modulated by Redox State of HMGB1

0427973 - BFÚ 2015 RIV US eng J - Journal Article
Muselíková Polanská, Eva - Pospíšilová, Š. - Štros, Michal
Binding of Histone H1 to DNA Is Differentially Modulated by Redox State of HMGB1.
PLoS ONE. Roč. 9, č. 2 (2014). ISSN 1932-6203. E-ISSN 1932-6203
R&D Projects: GA ČR(CZ) GAP305/12/2475; GA MŠMT(CZ) ED1.1.00/02.0068
Institutional support: RVO:68081707
Keywords : CHROMOSOMAL-PROTEIN HMG1 * MOBILITY GROUP-1 PROTEIN * LINKER HISTONES
Subject RIV: BO - Biophysics
Impact factor: 3.234, year: 2014

HMGB1 is an architectural protein in chromatin, acting also as a signaling molecule outside the cell. Recent reports from several laboratories provided evidence that a number of both the intracellular and extracellular functions of HMGB1 may depend on redox-sensitive cysteine residues of the protein. In this study we demonstrate that redox state of HMGB1 can significantly modulate the ability of the protein to bind and bend DNA, as well as to promote DNA end-joining. We also report a high affinity binding of histone H1 to hemicatenated DNA loops and DNA minicircles. Finally, we show that reduced HMGB1 can readily displace histone H1 from DNA, while oxidized HMGB1 has limited capacity for H1 displacement. Our results suggested a novel mechanism for the HMGB1-mediated modulation of histone H1 binding to DNA. Possible biological consequences of linker histones H1 replacement by HMGB1 for the functioning of chromatin are discussed.
Permanent Link: http://hdl.handle.net/11104/0233413