N-Terminal Domain of Nuclear IL-1 alpha Shows Structural Similarity to the C-Terminal Domain of Snf1 and Binds to the HAT/Core Module of the SAGA Complex

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10131045" target="_blank" >RIV/00216208:11310/12:10131045 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1371/journal.pone.0041801" target="_blank" >http://dx.doi.org/10.1371/journal.pone.0041801</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1371/journal.pone.0041801" target="_blank" >10.1371/journal.pone.0041801</a>

Jazyk výsledku

angličtina

Název v původním jazyce

N-Terminal Domain of Nuclear IL-1 alpha Shows Structural Similarity to the C-Terminal Domain of Snf1 and Binds to the HAT/Core Module of the SAGA Complex

Popis výsledku v původním jazyce

Interleukin-1 alpha (IL-1 alpha) is a proinflammatory cytokine and a key player in host immune responses in higher eukaryotes. IL-1 alpha has pleiotropic effects on a wide range of cell types, and it has been extensively studied for its ability to contribute to various autoimmune and inflammation-linked disorders, including rheumatoid arthritis, Alzheimer's disease, systemic sclerosis and cardiovascular disorders. Interestingly, a significant proportion of IL-1 alpha is translocated to the cell nucleus,in which it interacts with histone acetyltransferase complexes. Despite the importance of IL-1 alpha, little is known regarding its binding targets and functions in the nucleus. We took advantage of the histone acetyltransferase (HAT) complexes being evolutionarily conserved from yeast to humans and the yeast SAGA complex serving as an epitome of the eukaryotic HAT complexes. Using gene knock-out technique and co-immunoprecipitation of the IL-1 alpha precursor with TAP-tagged subunits o

Název v anglickém jazyce

N-Terminal Domain of Nuclear IL-1 alpha Shows Structural Similarity to the C-Terminal Domain of Snf1 and Binds to the HAT/Core Module of the SAGA Complex

Popis výsledku anglicky

Interleukin-1 alpha (IL-1 alpha) is a proinflammatory cytokine and a key player in host immune responses in higher eukaryotes. IL-1 alpha has pleiotropic effects on a wide range of cell types, and it has been extensively studied for its ability to contribute to various autoimmune and inflammation-linked disorders, including rheumatoid arthritis, Alzheimer's disease, systemic sclerosis and cardiovascular disorders. Interestingly, a significant proportion of IL-1 alpha is translocated to the cell nucleus,in which it interacts with histone acetyltransferase complexes. Despite the importance of IL-1 alpha, little is known regarding its binding targets and functions in the nucleus. We took advantage of the histone acetyltransferase (HAT) complexes being evolutionarily conserved from yeast to humans and the yeast SAGA complex serving as an epitome of the eukaryotic HAT complexes. Using gene knock-out technique and co-immunoprecipitation of the IL-1 alpha precursor with TAP-tagged subunits o

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

<a href="/cs/project/NS9819" target="_blank" >NS9819: Význam interakce nádorového supresoru p53 a interleukinu-1alfa při nádorové transformaci</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

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

7

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

12

Strana od-do

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Kód UT WoS článku

000307810000010

EID výsledku v databázi Scopus

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