Fiche publication
Date publication
octobre 2024
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Pr MOTORINE Iouri
,
Dr MARCHAND Virginie
Tous les auteurs :
Dominique C, Maiga NK, Méndez-Godoy A, Pillet B, Hamze H, Léger-Silvestre I, Henry Y, Marchand V, Gomes Neto V, Dez C, Motorin Y, Kressler D, Gadal O, Henras AK, Albert B
Lien Pubmed
Résumé
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.
Mots clés
Saccharomyces cerevisiae, metabolism, Lysine, metabolism, Cell Nucleolus, metabolism, RNA, Ribosomal, metabolism, Saccharomyces cerevisiae Proteins, metabolism, Ribonucleoproteins, Small Nucleolar, metabolism, Ribosomes, metabolism, Protein Domains, RNA Polymerase I, metabolism, Intrinsically Disordered Proteins, metabolism, Humans
Référence
Nat Commun. 2024 10 31;15(1):9415
