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

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...

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Published in:Cells (Basel, Switzerland) Switzerland), 2020-05, Vol.9 (5), p.1143
Main Authors: Guillen-Chable, Francisco, Corona, Ulises Rodríguez, Pereira-Santana, Alejandro, Bayona, Andrea, Rodríguez-Zapata, Luis Carlos, Aquino, Cecilia, Šebestová, Lenka, Vitale, Nicolas, Hozak, Pavel, Castano, Enrique
Format: Article
Language:English
Subjects:
Chromosomal Proteins, Non-Histone - chemistry
Chromosomal Proteins, Non-Histone - genetics
Chromosomal Proteins, Non-Histone - metabolism
fibrillarin
HeLa Cells
Humans
Life Sciences
Mutation - genetics
Neurons and Cognition
nucleolus
phosphoinositides
Phospholipids - metabolism
Protein Domains
Recombinant Proteins - metabolism
Ribonucleases - chemistry
Ribonucleases - genetics
Ribonucleases - metabolism
ribonucleolar particle
Ribonucleoproteins - metabolism
RNA, Small Nucleolar - metabolism
rRNA
Structure-Activity Relationship
viral progression
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Summary: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.
ISSN:2073-4409
2073-4409
DOI:10.3390/cells9051143