Binding of histone H1 to DNA is differentially modulated by
redox state of HMGB1

J 2014

Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1

POLANSKÁ, Eva, Šárka POSPÍŠILOVÁ a Michal ŠTROS

Základní údaje

Originální název

Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1

Autoři

POLANSKÁ, Eva (203 Česká republika), Šárka POSPÍŠILOVÁ (203 Česká republika, garant, domácí) a Michal ŠTROS (203 Česká republika, domácí)

Vydání

Plos one, San Francisco, Public Library Science, 2014, 1932-6203

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

30200 3.2 Clinical medicine

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.234

Kód RIV

RIV/00216224:14740/14:00074179

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1371/journal.pone.0089070

UT WoS

000331266000098

Klíčová slova anglicky

HMGB1; chromatin; DNA

Štítky

kontrola MP, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 6. 3. 2015 08:38, Martina Prášilová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

GAP305/12/2475, projekt VaV

Název: Proteiny HMGB: funkce v biologii telomer a lidských embryonálních kmenových buněk

Investor: Grantová agentura ČR, Proteiny HMGB: funkce v biologii telomer a lidských embryonálních kmenových buněk

286154, interní kód MU

Název: SYLICA - Synergies of Life and Material Sciences to Create a New Future (Akronym: SYLICA)

Investor: Evropská unie, SYLICA - Synergies of Life and Material Sciences to Create a New Future, Kapacity

Citovat

POLANSKÁ, Eva, Šárka POSPÍŠILOVÁ a Michal ŠTROS. Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1. Plos one. San Francisco: Public Library Science, 2014, roč. 9, č. 2, s. "nestránkováno", 10 s. ISSN 1932-6203. Dostupné z: https://dx.doi.org/10.1371/journal.pone.0089070.

@article{1212583,
   author = {Polanská, Eva and Pospíšilová, Šárka and Štros, Michal},
   article_location = {San Francisco},
   article_number = {2},
   doi = {http://dx.doi.org/10.1371/journal.pone.0089070},
   keywords = {HMGB1; chromatin; DNA},
   language = {eng},
   issn = {1932-6203},
   journal = {Plos one},
   title = {Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1},
   url = {http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0089070},
   volume = {9},
   year = {2014}
}

TY  - JOUR
ID  - 1212583
AU  - Polanská, Eva - Pospíšilová, Šárka - Štros, Michal
PY  - 2014
TI  - Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1
JF  - Plos one
VL  - 9
IS  - 2
SP  - "nestránkováno"
EP  - "nestránkováno"
PB  - Public Library Science
SN  - 19326203
KW  - HMGB1
KW  - chromatin
KW  - DNA
UR  - http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0089070
L2  - http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0089070
N2  - 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.
ER  -

POLANSKÁ, Eva, Šárka POSPÍŠILOVÁ a Michal ŠTROS. Binding of histone H1 to DNA is differentially modulated by redox state of HMGB1. \textit{Plos one}. San Francisco: Public Library Science, 2014, roč.~9, č.~2, s.~''nestránkováno'', 10 s. ISSN~1932-6203. Dostupné z: https://dx.doi.org/10.1371/journal.pone.0089070.

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