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Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases

Author

Listed:
  • Urszula M. McCaughan

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Uma Jayachandran

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Vadim Shchepachev

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Zhuo Angel Chen

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Juri Rappsilber

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh
    Institute of Biotechnology, Technische Universität Berlin)

  • David Tollervey

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

  • Atlanta G. Cook

    (Wellcome Trust Centre for Cell Biology, University of Edinburgh)

Abstract

Budding yeast Tsr1 is a ribosome biogenesis factor with sequence similarity to GTPases, which is essential for cytoplasmic steps in 40S subunit maturation. Here we present the crystal structure of Tsr1 at 3.6 Å. Tsr1 has a similar domain architecture to translational GTPases such as EF-Tu and the selenocysteine incorporation factor SelB. However, active site residues required for GTP binding and hydrolysis are absent, explaining the lack of enzymatic activity in previous analyses. Modelling of Tsr1 into cryo-electron microscopy maps of pre-40S particles shows that a highly acidic surface of Tsr1 is presented on the outside of pre-40S particles, potentially preventing premature binding to 60S subunits. Late pre-40S maturation also requires the GTPase eIF5B and the ATPase Rio1. The location of Tsr1 is predicted to block binding by both factors, strongly indicating that removal of Tsr1 is an essential step during cytoplasmic maturation of 40S ribosomal subunits.

Suggested Citation

  • Urszula M. McCaughan & Uma Jayachandran & Vadim Shchepachev & Zhuo Angel Chen & Juri Rappsilber & David Tollervey & Atlanta G. Cook, 2016. "Pre-40S ribosome biogenesis factor Tsr1 is an inactive structural mimic of translational GTPases," Nature Communications, Nature, vol. 7(1), pages 1-8, September.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms11789
    DOI: 10.1038/ncomms11789
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