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Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1
E. Polanská, Š. Pospíšilová, M. Štros,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2006
Free Medical Journals
od 2006
Public Library of Science (PLoS)
od 2006
PubMed Central
od 2006
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od 2006
ProQuest Central
od 2006-12-01
Open Access Digital Library
od 2006-01-01
Open Access Digital Library
od 2006-10-01
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od 2006-01-01
Medline Complete (EBSCOhost)
od 2008-01-01
Nursing & Allied Health Database (ProQuest)
od 2006-12-01
Health & Medicine (ProQuest)
od 2006-12-01
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ROAD: Directory of Open Access Scholarly Resources
od 2006
- MeSH
- chromatin genetika metabolismus MeSH
- exprese genu MeSH
- genetické vektory chemie MeSH
- histony genetika metabolismus MeSH
- konkatenovaná DNA genetika metabolismus MeSH
- kruhová DNA genetika metabolismus MeSH
- krysa rodu rattus MeSH
- lidé MeSH
- oxidace-redukce MeSH
- protein HMGB1 genetika metabolismus MeSH
- rekombinantní proteiny genetika metabolismus MeSH
- skot MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- krysa rodu rattus MeSH
- lidé MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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.
Citace poskytuje Crossref.org
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