ArticleNature communications2024
The dual life of disordered lysine-rich domains of snoRNPs in rRNA modification and nucleolar compaction.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- CPF-CF-terminated snoRNAs shuttle through the cytoplasm via an mRNA guard protein-mediated surveillance mechanism.Nature communications · 2026Article
- Intrinsically disordered regions stimulate concentration of small nucleolar ribonucleoproteins and formation of Cajal bodies and nucleoli.Genes & development · 2026Article
- Fibrillarin/Nop1 perturbs RNA folding and assembly independently of liquid-liquid phase separation.Nucleic acids research · 2026Article
- Biomolecular Condensates Can Induce Local Membrane Potentials.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Systematic mapping of small nucleolar RNA interactions in human cells.RNA biology · 2025Article
- New insights into nuclear import and nucleolar localization of yeast RNA exosome subunits.Molecular biology of the cell · 2025Article
- The snoRNP chaperone snR190 and the Npa1 complex form a macromolecular assembly required for 60S ribosomal subunit maturation.Nucleic acids research · 2025Article
- RNA-Protein Assemblies: A Review of Biophysical Principles and Coarse-Grained Modeling Approaches.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
15 authors.
Funding
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.
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