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.

Biochemistry and Molecular Plant Biology Department Centro de Investigación Científica de Yucatán A C Calle 43 No 130 Colonia Chuburná de Hidalgo Mérida C P 97200 Yucatán Mexico

Biotechnology Department Centro de Investigación Científica de Yucatán A C Calle 43 No 130 Colonia Chuburná de Hidalgo Mérida C P 97200 Yucatan Mexico

Department of Biology of the Cell Nucleus Institute of Molecular Genetics of the CAS v v i Videnska 1083 142 20 Prague Czech Republic

Dirección de Cátedras Consejo Nacional de Ciencia y Tecnología Av Insurgentes Sur 1582 Alcaldia Benito Juarez C P 03940 Ciudad de Mexico Mexico

Faculty of Science Charles University Albertov 6 128 00 Prague Czech Republic

Industrial Biotechnology Department Centro de Investigación y Asistencia en Tecnología y Diseño del Estado de Jalisco A C Camino Arenero 1227 el Bajio Zapopan C P 45019 Jalisco Mexico

Institute of Celullar and Integrative Neuroscience UPR 3212 The French National Centre for Scientific Research and University of Strasbourg 67000 Strasbourg France

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Dual-color dSTORM imaging and ThunderSTORM image reconstruction and analysis to study the spatial organization of the nuclear phosphatidylinositol phosphates

Limited Proteolysis-Coupled Mass Spectrometry Identifies Phosphatidylinositol 4,5-Bisphosphate Effectors in Human Nuclear Proteome