Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F14%3A00074179" target="_blank" >RIV/00216224:14740/14:00074179 - isvavai.cz</a>
Alternative codes found
RIV/68081707:_____/14:00427973
Result on the web
<a href="http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0089070" target="_blank" >http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0089070</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0089070" target="_blank" >10.1371/journal.pone.0089070</a>
Alternative languages
Result language
angličtina
Original language name
Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1
Original language description
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 theHMGB1-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.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
FD - Oncology and haematology
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Plos one
ISSN
1932-6203
e-ISSN
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Volume of the periodical
9
Issue of the periodical within the volume
2
Country of publishing house
US - UNITED STATES
Number of pages
10
Pages from-to
"nestránkováno"
UT code for WoS article
000331266000098
EID of the result in the Scopus database
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