Cells (May 2020)

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

  • Francisco Guillen-Chable,
  • Ulises Rodríguez Corona,
  • Alejandro Pereira-Santana,
  • Andrea Bayona,
  • Luis Carlos Rodríguez-Zapata,
  • Cecilia Aquino,
  • Lenka Šebestová,
  • Nicolas Vitale,
  • Pavel Hozak,
  • Enrique Castano

DOI
https://doi.org/10.3390/cells9051143
Journal volume & issue
Vol. 9, no. 5
p. 1143

Abstract

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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.

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