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High-throughput RNA structure probing reveals critical folding events during early 60S ribosome assembly in yeast

Author

Listed:
  • Elena Burlacu

    (University of Edinburgh)

  • Fredrik Lackmann

    (The Wenner-Gren Institute, Stockholm University)

  • Lisbeth-Carolina Aguilar

    (Systems Biology Axis)

  • Sergey Belikov

    (The Wenner-Gren Institute, Stockholm University)

  • Rob van Nues

    (Institute of Cell Biology, University of Edinburgh)

  • Christian Trahan

    (Systems Biology Axis
    Université de Montréal Département de Biochimie et Médecine Moléculaire Faculté de Médecine)

  • Ralph D. Hector

    (Institute of Neuroscience and Psychology, University of Glasgow)

  • Nicholas Dominelli-Whiteley

    (EaStCHEM School of Chemistry, University of Edinburgh)

  • Scott L. Cockroft

    (EaStCHEM School of Chemistry, University of Edinburgh)

  • Lars Wieslander

    (The Wenner-Gren Institute, Stockholm University)

  • Marlene Oeffinger

    (Systems Biology Axis
    Université de Montréal Département de Biochimie et Médecine Moléculaire Faculté de Médecine
    McGill University Division of Experimental Medicine Department of medicine)

  • Sander Granneman

    (University of Edinburgh)

Abstract

While the protein composition of various yeast 60S ribosomal subunit assembly intermediates has been studied in detail, little is known about ribosomal RNA (rRNA) structural rearrangements that take place during early 60S assembly steps. Using a high-throughput RNA structure probing method, we provide nucleotide resolution insights into rRNA structural rearrangements during nucleolar 60S assembly. Our results suggest that many rRNA-folding steps, such as folding of 5.8S rRNA, occur at a very specific stage of assembly, and propose that downstream nuclear assembly events can only continue once 5.8S folding has been completed. Our maps of nucleotide flexibility enable making predictions about the establishment of protein–rRNA interactions, providing intriguing insights into the temporal order of protein–rRNA as well as long-range inter-domain rRNA interactions. These data argue that many distant domains in the rRNA can assemble simultaneously during early 60S assembly and underscore the enormous complexity of 60S synthesis.

Suggested Citation

  • Elena Burlacu & Fredrik Lackmann & Lisbeth-Carolina Aguilar & Sergey Belikov & Rob van Nues & Christian Trahan & Ralph D. Hector & Nicholas Dominelli-Whiteley & Scott L. Cockroft & Lars Wieslander & M, 2017. "High-throughput RNA structure probing reveals critical folding events during early 60S ribosome assembly in yeast," Nature Communications, Nature, vol. 8(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00761-8
    DOI: 10.1038/s41467-017-00761-8
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    Cited by:

    1. Gerald Ryan R. Aquino & Philipp Hackert & Nicolai Krogh & Kuan-Ting Pan & Mariam Jaafar & Anthony K. Henras & Henrik Nielsen & Henning Urlaub & Katherine E. Bohnsack & Markus T. Bohnsack, 2021. "The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly," Nature Communications, Nature, vol. 12(1), pages 1-16, December.
    2. Mariam Jaafar & Julia Contreras & Carine Dominique & Sara Martín-Villanueva & Régine Capeyrou & Patrice Vitali & Olga Rodríguez-Galán & Carmen Velasco & Odile Humbert & Nicholas J. Watkins & Eduardo V, 2021. "Association of snR190 snoRNA chaperone with early pre-60S particles is regulated by the RNA helicase Dbp7 in yeast," Nature Communications, Nature, vol. 12(1), pages 1-17, December.

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