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RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes.

Lukas Brüning1, Philipp Hackert1, Roman Martin1

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This study reveals how three RNA helicases, Has1, Mak5, and Spb4, orchestrate key events in eukaryotic ribosome biogenesis. Their specific binding sites guide structural rearrangements, ensuring accurate assembly of ribosomal subunits for protein synthesis.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Eukaryotic ribosome biogenesis is a complex, dynamic process involving numerous structural rearrangements.
  • Ribosome assembly requires precise coordination of RNA-protein interactions and conformational changes.
  • Understanding the roles of accessory factors is crucial for elucidating assembly fidelity checkpoints.

Purpose of the Study:

  • To identify the in vivo binding sites of three key RNA helicases (Has1, Mak5, Spb4) within pre-ribosomal complexes.
  • To elucidate the specific functions of these RNA helicases in driving structural remodeling events during ribosome assembly.
  • To provide mechanistic insights into the roles of RNA helicases in ensuring the fidelity of eukaryotic ribosome biogenesis.

Main Methods:

  • In vivo crosslinking coupled with immunoprecipitation to map RNA helicase binding sites on pre-ribosomes.
  • Analysis of pre-ribosomal complexes to determine the impact of RNA helicase binding on assembly intermediates.
  • Biochemical assays to assess the functional consequences of RNA helicase activity on ribosome subunit maturation and export.

Main Results:

  • Has1 binds to early 40S pre-ribosomes, facilitating U14 snoRNP release, and to pre-60S complexes, driving domain I assembly.
  • Mak5 binds to domain II of pre-60S complexes, promoting the recruitment of ribosomal protein Rpl10, essential for subunit joining.
  • Spb4 binds to ES27, facilitating Arx1 binding and promoting pre-60S export competence.

Conclusions:

  • Has1, Mak5, and Spb4 act at distinct stages and locations within the ribosome assembly pathway.
  • These RNA helicases play critical roles in driving specific structural rearrangements and facilitating the recruitment of other factors.
  • The findings illuminate the molecular mechanisms underlying the fidelity and efficiency of eukaryotic ribosome biogenesis.