The dual life of disordered lysine-rich domains of snoRNPs in rRNA modification and nucleolar compaction

Carine Dominique, Nana Kadidia Maiga, Alfonso Méndez-Godoy, Benjamin Pillet, Hussein Hamze, Isabelle Léger-Silvestre, Yves Henry, Virginie Marchand, Valdir Gomes Neto, Christophe Dez, Yuri Motorin, Dieter Kressler (), Olivier Gadal (), Anthony K. Henras () and Benjamin Albert ()
Additional contact information
Carine Dominique: UPS
Nana Kadidia Maiga: UPS
Alfonso Méndez-Godoy: University of Fribourg
Benjamin Pillet: University of Fribourg
Hussein Hamze: UPS
Isabelle Léger-Silvestre: UPS
Yves Henry: UPS
Virginie Marchand: UAR2008 IBSLor/UMR7365 IMoPA
Valdir Gomes Neto: University of São Paulo
Christophe Dez: UPS
Yuri Motorin: UAR2008 IBSLor/UMR7365 IMoPA
Dieter Kressler: University of Fribourg
Olivier Gadal: UPS
Anthony K. Henras: UPS
Benjamin Albert: UPS

Nature Communications, 2024, vol. 15, issue 1, 1-19

Abstract: Abstract Intrinsically disordered regions (IDRs) are highly enriched in the nucleolar proteome but their physiological role in ribosome assembly remains poorly understood. Our study reveals the functional plasticity of the extremely abundant lysine-rich IDRs of small nucleolar ribonucleoprotein particles (snoRNPs) from protists to mammalian cells. We show in Saccharomyces cerevisiae that the electrostatic properties of this lysine-rich IDR, the KKE/D domain, promote snoRNP accumulation in the vicinity of nascent rRNAs, facilitating their modification. Under stress conditions reducing the rate of ribosome assembly, they are essential for nucleolar compaction and sequestration of key early-acting ribosome biogenesis factors, including RNA polymerase I, owing to their self-interaction capacity in a latent, non-rRNA-associated state. We propose that such functional plasticity of these lysine-rich IDRs may represent an ancestral eukaryotic regulatory mechanism, explaining how nucleolar morphology is continuously adapted to rRNA production levels.

Date: 2024
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DOI: 10.1038/s41467-024-53805-1

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