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

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.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Michael Stumpe

LAB HEAD: Dieter Kressler

PROVIDER: PXD056946 | Pride | 2024-10-18

REPOSITORIES: Pride

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			Action	DRS
	20230703_MS_AMG_10564.raw	Raw
	20230703_MS_AMG_10565.raw	Raw
	20230703_MS_AMG_10566.raw	Raw
	20230703_MS_AMG_10570.raw	Raw
	20230703_MS_AMG_10571.raw	Raw

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