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TitleThe intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling.
Journal, issue, pagesNucleic Acids Res, Vol. 50, Issue 5, Page 2938-2958, Year 2022
Publish dateMar 21, 2022
AuthorsAlexandra Bergfort / Tarek Hilal / Benno Kuropka / İbrahim Avşar Ilik / Gert Weber / Tuğçe Aktaş / Christian Freund / Markus C Wahl /
PubMed AbstractBiogenesis of spliceosomal small nuclear ribonucleoproteins (snRNPs) and their recycling after splicing require numerous assembly/recycling factors whose modes of action are often poorly understood. ...Biogenesis of spliceosomal small nuclear ribonucleoproteins (snRNPs) and their recycling after splicing require numerous assembly/recycling factors whose modes of action are often poorly understood. The intrinsically disordered TSSC4 protein has been identified as a nuclear-localized U5 snRNP and U4/U6-U5 tri-snRNP assembly/recycling factor, but how TSSC4's intrinsic disorder supports TSSC4 functions remains unknown. Using diverse interaction assays and cryogenic electron microscopy-based structural analysis, we show that TSSC4 employs four conserved, non-contiguous regions to bind the PRPF8 Jab1/MPN domain and the SNRNP200 helicase at functionally important sites. It thereby inhibits SNRNP200 helicase activity, spatially aligns the proteins, coordinates formation of a U5 sub-module and transiently blocks premature interaction of SNRNP200 with at least three other spliceosomal factors. Guided by the structure, we designed a TSSC4 variant that lacks stable binding to the PRPF8 Jab1/MPN domain or SNRNP200 in vitro. Comparative immunoprecipitation/mass spectrometry from HEK293 nuclear extract revealed distinct interaction profiles of wild type TSSC4 and the variant deficient in PRPF8/SNRNP200 binding with snRNP proteins, other spliceosomal proteins as well as snRNP assembly/recycling factors and chaperones. Our findings elucidate molecular strategies employed by an intrinsically disordered protein to promote snRNP assembly, and suggest multiple TSSC4-dependent stages during snRNP assembly/recycling.
External linksNucleic Acids Res / PubMed:35188580 / PubMed Central
MethodsEM (single particle)
Resolution2.76 - 3.3 Å
Structure data

13045

7os1

EMDB-13045, PDB-7os1:
Cryo-EM structure of Brr2 in complex with Fbp21
Method: EM (single particle) / Resolution: 3.3 Å

13046

7os2

EMDB-13046, PDB-7os2:
Cryo-EM structure of Brr2 in complex with Jab1/MPN and C9ORF78
Method: EM (single particle) / Resolution: 2.76 Å

13690

7px3

EMDB-13690, PDB-7px3:
Structure of U5 snRNP assembly and recycling factor TSSC4 in complex with BRR2 and Jab1 domain of PRPF8
Method: EM (single particle) / Resolution: 3.05 Å

Source
  • homo sapiens (human)
KeywordsSPLICING / mRNA Splicing / Spliceosomal Assembly / Splicing Regulation / Brr2 Helicase / Spliceosomal biogenesis

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