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

0538155 - ÚMG 2021 RIV CH eng J - Journal Article
Guillen-Chable, F. - Rodriguez Corona, U. - Pereira-Santana, A. - Bayona, A. - Carlos Rodriguez-Zapata, L. - Aquino, C. - Šebestová, Lenka - Vitale, N. - Hozák, Pavel - Castano, E.
Fibrillarin Ribonuclease Activity is Dependent on the GAR Domain and Modulated by Phospholipids.
Cells. Roč. 9, č. 5 (2020), č. článku 1143. E-ISSN 2073-4409
R&D Projects: GA ČR GA19-05608S; GA ČR(CZ) GA18-19714S; GA MŠMT LTC19048; GA MŠMT(CZ) ED1.1.00/02.0109; GA MŠMT(CZ) LM2018129; GA MŠMT(CZ) EF16_013/0001775
Institutional support: RVO:68378050
Keywords : nucleolus * ribonucleolar particle * rRNA * fibrillarin * phosphoinositides * viral progression
OECD category: Cell biology
Impact factor: 6.600, year: 2020
Method of publishing: Open access
https://www.mdpi.com/2073-4409/9/5/1143

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.
Permanent Link: http://hdl.handle.net/11104/0315977