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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Detalles Bibliográficos
Autores: Francisco Guillén-Chable, ULISES RODRIGUEZ CORONA, Alejandro Pereira-Santana, ANDREA BAYONA HERNANDEZ, Luis Carlos Rodríguez Zapata, Cecilia Aquino Perez, Lenka Šebestová, Nicolas Vitale, Pavel Hozak, Enrique Castaño de la Serna
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:México
Institución:Centro de Investigación Científica de Yucatán
Repositorio:Repositorio Institucional CICY
Idioma:inglés
OAI Identifier:oai:cicy.repositorioinstitucional.mx:1003/1822
Acceso en línea:http://cicy.repositorioinstitucional.mx/jspui/handle/1003/1822
Access Level:acceso abierto
Palabra clave:info:eu-repo/classification/Autores/NUCLEOLUS
info:eu-repo/classification/Autores/RIBONUCLEOLAR PARTICLE
info:eu-repo/classification/Autores/RRNA
info:eu-repo/classification/Autores/FIBRILLARIN
info:eu-repo/classification/Autores/PHOSPHOINOSITIDES
info:eu-repo/classification/Autores/VIRAL PROGRESSION
info:eu-repo/classification/cti/2
info:eu-repo/classification/cti/24
info:eu-repo/classification/cti/2415
info:eu-repo/classification/cti/241502
Descripción
Sumario: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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