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%2F00216208%3A11310%2F20%3A10442515" target="_blank" >RIV/00216208:11310/20:10442515 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/20:00538155
Result on the web
<a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=KV7XMDamBP" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=KV7XMDamBP</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
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10600 - Biological sciences
Result continuities
Project
<a href="/en/project/ED1.1.00%2F02.0109" target="_blank" >ED1.1.00/02.0109: Biotechnology and Biomedicine Centre of the Academy of Sciences and Charles University</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
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 [online]
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
2-s2.0-85084721024