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Interprotomer Communication and Functional Asymmetry in H/ACA snoRNPs.

Hemendra Singh Panwar1, Timothy John Vos2, Xiaoyan Xie1

  • 1Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Biorxiv : the Preprint Server for Biology
|June 12, 2025
PubMed
Summary

H/ACA small nucleolar ribonucleoproteins (H/ACA snoRNPs) are crucial for RNA modification and stability. This study reveals their asymmetric dimeric structure, explaining pseudouridylation activity and offering insights into Dyskeratosis congenita.

Keywords:
RNA modificationguide RNApseudouridineribosome assemblytelomerase

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genetics

Background:

  • H/ACA small nucleolar ribonucleoproteins (H/ACA snoRNPs) are essential for RNA modification, folding, and stability, playing key roles in ribosome biogenesis and telomere maintenance.
  • Mutations in H/ACA snoRNP proteins are linked to the genetic disorder Dyskeratosis congenita, highlighting their clinical significance.
  • Eukaryotic H/ACA snoRNAs typically feature two hairpin structures, but the structural basis for this preference and its relation to function remained unclear.

Purpose of the Study:

  • To elucidate the structure and function of endogenous, catalytically active insect H/ACA snoRNPs.
  • To characterize the protein-protein and protein-RNA interactions within the H/ACA snoRNP complex.
  • To investigate the impact of Dyskeratosis congenita-associated mutations on H/ACA snoRNP activity and pseudouridine formation.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) to determine high-resolution structures of H/ACA snoRNPs.
  • Biochemical assays to characterize protein-protein and protein-RNA interactions.
  • Analysis of mutations associated with Dyskeratosis congenita to understand their functional consequences.

Main Results:

  • Multiple cryo-EM structures revealed an asymmetric, dimeric H/ACA snoRNP complex with two protomers bound to a two-hairpin snoRNA.
  • Key inter-protomer contact sites were identified, explaining the coordination of pseudouridylation activity and the prevalence of two-hairpin snoRNA structures.
  • Mutations in H/ACA proteins linked to Dyskeratosis congenita were found to impair pseudouridine formation, providing mechanistic insight into the disease.
  • Coordinated structural changes in specific H/ACA subunits suggest a regulatory mechanism for snoRNP activity.

Conclusions:

  • The study provides unprecedented structural detail of active H/ACA snoRNPs, revealing an asymmetric dimeric architecture.
  • The findings elucidate the mechanism of coordinated pseudouridylation and shed light on the pathogenesis of Dyskeratosis congenita.
  • This work deepens the understanding of H/ACA snoRNP function in critical cellular processes, including RNA modification, ribosome biogenesis, and telomere maintenance.