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H/ACA snR30 snoRNP guides independent 18S rRNA subdomain formation

Author

Listed:
  • Paulina Fischer

    (Heidelberg University)

  • Matthias Thoms

    (University of Munich)

  • Benjamin Lau

    (Heidelberg University
    European Molecular Biology Laboratory (EMBL))

  • Timo Denk

    (University of Munich)

  • Maria Kuvshinova

    (Heidelberg University)

  • Otto Berninghausen

    (University of Munich)

  • Dirk Flemming

    (Heidelberg University)

  • Ed Hurt

    (Heidelberg University)

  • Roland Beckmann

    (University of Munich)

Abstract

Ribosome biogenesis follows a cascade of pre-rRNA folding and processing steps, coordinated with ribosomal protein incorporation. Nucleolar 90S pre-ribosomes are well-described stable intermediates, composed of pre-18S rRNA, ribosomal S-proteins, U3 snoRNA, and ~70 assembly factors. However, how numerous snoRNAs control pre-rRNA modification and folding during early maturation events remains unclear. We identify snR30 (human U17), the only essential H/ACA snoRNA in yeast, which binds with Cbf5-Gar1-Nop10-Nhp2 to a pre-18S rRNA subdomain containing platform helices and ES6 of the 40S central domain. Integration into the 90S is blocked by RNA hybridization with snR30. The snoRNP complex coordinates the recruitment of early assembly factors Krr1-Utp23-Kri1 and ribosomal proteins uS11-uS15, enabling isolated subdomain assembly. Krr1-dependent release of snR30 culminates in integration of the platform into the 90S. Our study reveals the essential role of snR30 in chaperoning central domain formation as a discrete assembly unit externalized from the pre-ribosomal core.

Suggested Citation

  • Paulina Fischer & Matthias Thoms & Benjamin Lau & Timo Denk & Maria Kuvshinova & Otto Berninghausen & Dirk Flemming & Ed Hurt & Roland Beckmann, 2025. "H/ACA snR30 snoRNP guides independent 18S rRNA subdomain formation," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-59656-8
    DOI: 10.1038/s41467-025-59656-8
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