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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

The result's identifiers

  • Result code in 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>

  • Result on the web

    <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>

Alternative languages

  • Result language

    angličtina

  • Original language name

    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

  • Original language description

    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

  • Czech name

  • Czech description

Classification

  • Type

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

  • CEP classification

    EB - Genetics and molecular biology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/NS9819" target="_blank" >NS9819: The role of the interaction of the p53 tumour supressor and interleukin-1alpha in malignant transformation</a><br>

  • Continuities

    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

Others

  • Publication year

    2012

  • 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

    7

  • Issue of the periodical within the volume

    8

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    12

  • Pages from-to

  • UT code for WoS article

    000307810000010

  • EID of the result in the Scopus database