Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00081255" target="_blank" >RIV/00216224:14740/15:00081255 - isvavai.cz</a>
Alternative codes found
RIV/68081707:_____/15:00456700
Result on the web
<a href="http://www.plosone.org/article/fetchObject.action?uri=info:doi/10.1371/journal.pone.0138774&representation=PDF" target="_blank" >http://www.plosone.org/article/fetchObject.action?uri=info:doi/10.1371/journal.pone.0138774&representation=PDF</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1371/journal.pone.0138774" target="_blank" >10.1371/journal.pone.0138774</a>
Alternative languages
Result language
angličtina
Original language name
Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein
Original language description
HMGB1 protein and linker histone H1 have overlapping binding sites in the nucleosome. HMGB1 has been implicated in many DNA-dependent processes in chromatin involving binding of specific proteins, including transcription factors, to DNA sites pre-bent byHMGB1. HMGB1 can also act as an extracellular signaling molecule by promoting inflammation, tumor growth a metastasis. Many of the intra-and extracellular functions of HMGB1 depend on redox-sensitive cysteine residues of the protein. Here we report thatmild oxidization of HMGB1 (and much less mutation of cysteines involved in disulphide bond formation) can severely compromise the functioning of the protein as a DNA chaperone by inhibiting its ability to unwind or bend DNA. Histone H1 (via the highly basic C-terminal domain) significantly inhibits DNA bending by the full-length HMGB1, and the inhibition is further enhanced upon oxidization of HMGB1.
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
CE - Biochemistry
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
2015
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
10
Issue of the periodical within the volume
9
Country of publishing house
US - UNITED STATES
Number of pages
20
Pages from-to
"nestránkováno"
UT code for WoS article
000361800700093
EID of the result in the Scopus database
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