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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

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

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

  • 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