40S hnRNP particles are a novel class of nuclear biomolecular condensates.

Domanski, Michal; Dedic, Emil; Pérez, Maria Escura; Cléry, Antoine; Campagne, Sébastien; Uldry, Anne-Christine; Braga, Sophie; Heller, Manfred; Rabl, Julius; Afanasyev, Pavel; Boehringer, Daniel; Nováček, Jiří; Allain, Frédéric T; Mühlemann, Oliver (2022). 40S hnRNP particles are a novel class of nuclear biomolecular condensates. Nucleic acids research, 50(11), pp. 6300-6312. Oxford University Press 10.1093/nar/gkac457

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Heterogenous nuclear ribonucleoproteins (hnRNPs) are abundant proteins implicated in various steps of RNA processing that assemble on nuclear RNA into larger complexes termed 40S hnRNP particles. Despite their initial discovery 55 years ago, our understanding of these intriguing macromolecular assemblies remains limited. Here, we report the biochemical purification of native 40S hnRNP particles and the determination of their complete protein composition by label-free quantitative mass spectrometry, identifying A-group and C-group hnRNPs as the major protein constituents. Isolated 40S hnRNP particles dissociate upon RNA digestion and can be reconstituted in vitro on defined RNAs in the presence of the individual protein components, demonstrating a scaffolding role for RNA in nucleating particle formation. Finally, we revealed their nanometer scale, condensate-like nature, promoted by intrinsically disordered regions of A-group hnRNPs. Collectively, we identify nuclear 40S hnRNP particles as novel dynamic biomolecular condensates.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Chemistry, Biochemistry and Pharmaceutical Sciences (DCBP)
04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > DCR Services > Core Facility Massenspektrometrie- und Proteomics-Labor

UniBE Contributor:

Domanski, Michal, Uldry, Anne-Christine, Braga, Sophie Marie-Pierre, Heller, Manfred, Mühlemann, Oliver

Subjects:

500 Science > 540 Chemistry

ISSN:

0305-1048

Publisher:

Oxford University Press

Language:

English

Submitter:

Pubmed Import

Date Deposited:

13 Jun 2022 07:42

Last Modified:

05 Dec 2022 16:20

Publisher DOI:

10.1093/nar/gkac457

PubMed ID:

35687109

BORIS DOI:

10.48350/170581

URI:

https://boris.unibe.ch/id/eprint/170581

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