TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation

Klára Klimešová, Jitka Vojáčková, Nenad Radivojević, Franck Vandermoere, Edouard Bertrand, Celine Verheggen and David Staněk ()
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Klára Klimešová: Institute of Molecular Genetics, Czech Academy of Sciences
Jitka Vojáčková: Institute of Molecular Genetics, Czech Academy of Sciences
Nenad Radivojević: Institute of Molecular Genetics, Czech Academy of Sciences
Franck Vandermoere: Institut de Génomique Fonctionnelle, University of Montpellier, CNRS, INSERM
Edouard Bertrand: Institut de Génétique Moléculaire de Montpellier, University of Montpellier, CNRS
Celine Verheggen: Institut de Génétique Moléculaire de Montpellier, University of Montpellier, CNRS
David Staněk: Institute of Molecular Genetics, Czech Academy of Sciences

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract U5 snRNP is a complex particle essential for RNA splicing. U5 snRNPs undergo intricate biogenesis that ensures that only a fully mature particle assembles into a splicing competent U4/U6•U5 tri-snRNP and enters the splicing reaction. During splicing, U5 snRNP is substantially rearranged and leaves as a U5/PRPF19 post-splicing particle, which requires re-generation before the next round of splicing. Here, we show that a previously uncharacterized protein TSSC4 is a component of U5 snRNP that promotes tri-snRNP formation. We provide evidence that TSSC4 associates with U5 snRNP chaperones, U5 snRNP and the U5/PRPF19 particle. Specifically, TSSC4 interacts with U5-specific proteins PRPF8, EFTUD2 and SNRNP200. We also identified TSSC4 domains critical for the interaction with U5 snRNP and the PRPF19 complex, as well as for TSSC4 function in tri-snRNP assembly. TSSC4 emerges as a specific chaperone that acts in U5 snRNP de novo biogenesis as well as post-splicing recycling.

Date: 2021
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DOI: 10.1038/s41467-021-23934-y

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