DOMANSKI, Michal, Emil DEDIC, Maria Escura PEREZ, Antoine CLERY, Sebastien CAMPAGNE, Anne-Christine ULDRY, Sophie BRAGA, Manfred HELLER, Julius RABL, Pavel AFANASYEV, Daniel BOEHRINGER, Jiří NOVÁČEK, Frederic T ALLAIN and Oliver MUEHLEMANN. 40S hnRNP particles are a novel class of nuclear biomolecular condensates. Nucleic acids research. Oxford: Oxford University Press, 2022, vol. 50, No 11, p. 6300-6312. ISSN 0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkac457.
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Basic information
Original name 40S hnRNP particles are a novel class of nuclear biomolecular condensates
Authors DOMANSKI, Michal, Emil DEDIC, Maria Escura PEREZ, Antoine CLERY, Sebastien CAMPAGNE, Anne-Christine ULDRY, Sophie BRAGA, Manfred HELLER, Julius RABL, Pavel AFANASYEV, Daniel BOEHRINGER, Jiří NOVÁČEK (203 Czech Republic, guarantor, belonging to the institution), Frederic T ALLAIN and Oliver MUEHLEMANN.
Edition Nucleic acids research, Oxford, Oxford University Press, 2022, 0305-1048.
Other information
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher United Kingdom of Great Britain and Northern Ireland
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 14.900
RIV identification code RIV/00216224:14740/22:00128460
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1093/nar/gkac457
UT WoS 000809111100001
Keywords in English RNA-BINDING PROTEINSRIBONUCLEOPROTEIN COMPLEX HNRNPPHASE-SEPARATIONMESSENGER-RNASTRUCTURAL ORGANIZATIONLABEL-FREEA1IDENTIFICATIONPURIFICATIONNUCLEOTIDES
Tags rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 31/1/2023 15:43.
Abstract
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.
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