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

Nat Commun. 2018 Dec 19;9(1):5383. doi: 10.1038/s41467-018-07783-w.

Abstract

Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism
  • Binding Sites
  • DEAD-box RNA Helicases / metabolism*
  • Ribosomal Proteins / metabolism
  • Ribosome Subunits / metabolism*
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Arx1 protein, S cerevisiae
  • RPL10 protein, S cerevisiae
  • Ribosomal Proteins
  • Saccharomyces cerevisiae Proteins
  • Has1 protein, S cerevisiae
  • Adenosine Triphosphatases
  • MAK5 protein, S cerevisiae
  • SPB4 protein, S cerevisiae
  • DEAD-box RNA Helicases