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snoRNPs 中富含赖氨酸的结构域在 rRNA 修饰和核仁紧缩中的双重作用。

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

机构信息

Molecular, Cellular and Developmental (MCD) Unit, Centre for Integrative Biology (CBI), CNRS, University of Toulouse, UPS, Toulouse, France.

Department of Biology, University of Fribourg, Fribourg, Switzerland.

出版信息

Nat Commun. 2024 Oct 31;15(1):9415. doi: 10.1038/s41467-024-53805-1.

DOI:10.1038/s41467-024-53805-1
PMID:39482307
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11528048/
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.

摘要

无规则区域（IDR）在核仁蛋白质组中高度富集，但它们在核糖体组装中的生理作用仍知之甚少。我们的研究揭示了从原生生物到哺乳动物细胞中，小核仁核糖核蛋白颗粒（snoRNP）中极其丰富的富含赖氨酸的 IDR 的功能可塑性。我们在酿酒酵母中表明，这种富含赖氨酸的 IDR（KKE/D 结构域）的静电特性促进 snoRNP 在新生 rRNA 附近积累，从而促进其修饰。在降低核糖体组装速度的应激条件下，由于其在潜伏的、非 rRNA 相关状态下的自我相互作用能力，它们对于核仁的紧凑和关键早期作用的核糖体生物发生因子（包括 RNA 聚合酶 I）的隔离是必不可少的。我们提出，这些富含赖氨酸的 IDR 的这种功能可塑性可能代表了一种古老的真核调控机制，解释了核仁形态如何不断适应 rRNA 的产生水平。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/98734d9c9f46/41467_2024_53805_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/2a2a031beb5a/41467_2024_53805_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/2c0dbbefbb22/41467_2024_53805_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/abbcb60da3ec/41467_2024_53805_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/f3de9de694ae/41467_2024_53805_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/3eb0917a7b98/41467_2024_53805_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/596a28434141/41467_2024_53805_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/671a37df2588/41467_2024_53805_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/98734d9c9f46/41467_2024_53805_Fig8_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/2a2a031beb5a/41467_2024_53805_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/2c0dbbefbb22/41467_2024_53805_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/abbcb60da3ec/41467_2024_53805_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/f3de9de694ae/41467_2024_53805_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/3eb0917a7b98/41467_2024_53805_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/596a28434141/41467_2024_53805_Fig6_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/671a37df2588/41467_2024_53805_Fig7_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a5d4/11528048/98734d9c9f46/41467_2024_53805_Fig8_HTML.jpg

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