Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/68081707:_____/15:00456700

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Histone H1 Differentially Inhibits DNA Bending by Reduced and Oxidized HMGB1 Protein

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Plos one

ISSN

1932-6203

e-ISSN

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Svazek periodika

10

Číslo periodika v rámci svazku

9

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

20

Strana od-do

"nestránkováno"

Kód UT WoS článku

000361800700093

EID výsledku v databázi Scopus

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