UtpA and UtpB chaperone nascent pre-ribosomal RNA and U3 snoRNA to initiate eukaryotic ribosome assembly

Mirjam Hunziker, Jonas Barandun, Elisabeth Petfalski, Dongyan Tan, Clémentine Delan-Forino, Kelly R. Molloy, Kelly H. Kim, Hywel Dunn-Davies, Yi Shi, Malik Chaker-Margot, Brian T. Chait, Thomas Walz, David Tollervey, Sebastian Klinge*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Early eukaryotic ribosome biogenesis involves large multi-protein complexes, which co-transcriptionally associate with pre-ribosomal RNA to form the small subunit processome. The precise mechanisms by which two of the largest multi-protein complexes-UtpA and UtpB-interact with nascent pre-ribosomal RNA are poorly understood. Here, we combined biochemical and structural biology approaches with ensembles of RNA-protein cross-linking data to elucidate the essential functions of both complexes. We show that UtpA contains a large composite RNA-binding site and captures the 5′ end of pre-ribosomal RNA. UtpB forms an extended structure that binds early pre-ribosomal intermediates in close proximity to architectural sites such as an RNA duplex formed by the 5′ ETS and U3 snoRNA as well as the 3′ boundary of the 18S rRNA. Both complexes therefore act as vital RNA chaperones to initiate eukaryotic ribosome assembly.

Original languageEnglish
Article number12090
Number of pages10
JournalNature Communications
Volume7
DOIs
Publication statusPublished - 29 Jun 2016

Keywords

  • Chaperones
  • Ribosome
  • Supramolecular assembly

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