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Fibrillarin Ribonuclease Activity is Dependent on the GAR Domain and Modulated by Phospholipids

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F20%3A00538155" target="_blank" >RIV/68378050:_____/20:00538155 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/20:10442515

  • Result on the web

    <a href="https://www.mdpi.com/2073-4409/9/5/1143" target="_blank" >https://www.mdpi.com/2073-4409/9/5/1143</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/cells9051143" target="_blank" >10.3390/cells9051143</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Fibrillarin Ribonuclease Activity is Dependent on the GAR Domain and Modulated by Phospholipids

  • Original language description

    Fibrillarin is a highly conserved nucleolar methyltransferase responsible for ribosomal RNA methylation across evolution from Archaea to humans. It has been reported that fibrillarin is involved in the methylation of histone H2A in nucleoli and other processes, including viral progression, cellular stress, nuclear shape, and cell cycle progression. We show that fibrillarin has an additional activity as a ribonuclease. The activity is affected by phosphoinositides and phosphatidic acid and insensitive to ribonuclease inhibitors. Furthermore, the presence of phosphatidic acid releases the fibrillarin-U3 snoRNA complex. We show that the ribonuclease activity localizes to the GAR (glycine/arginine-rich) domain conserved in a small group of RNA interacting proteins. The introduction of the GAR domain occurred in evolution in the transition from archaea to eukaryotic cells. The interaction of this domain with phospholipids may allow a phase separation of this protein in nucleoli.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10601 - Cell biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

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

Data specific for result type

  • Name of the periodical

    Cells

  • ISSN

    2073-4409

  • e-ISSN

  • Volume of the periodical

    9

  • Issue of the periodical within the volume

    5

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    22

  • Pages from-to

    1143

  • UT code for WoS article

    000539340200077

  • EID of the result in the Scopus database