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Coupled GTPase and remodelling ATPase activities form a checkpoint for ribosome export

Author

Listed:
  • Yoshitaka Matsuo

    (Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany)

  • Sander Granneman

    (Wellcome Trust Centre for Cell Biology, The University of Edinburgh, Edinburgh EH9 3JR, UK
    Centre for Synthetic and Systems Biology, The University of Edinburgh, Edinburgh EH9 3JD, UK)

  • Matthias Thoms

    (Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany)

  • Rizos-Georgios Manikas

    (Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany)

  • David Tollervey

    (Wellcome Trust Centre for Cell Biology, The University of Edinburgh, Edinburgh EH9 3JR, UK)

  • Ed Hurt

    (Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany)

Abstract

Two proteins are identified in yeast that regulate the timing of pre-ribosome export from the nucleus; Nug2 binds pre-60S particles until they are ready for export, at which time Nug2 is replaced by the export adaptor Nmd3, enabling the export machinery to recognise the pre-ribosome that is ready to be transferred to the cytoplasm.

Suggested Citation

  • Yoshitaka Matsuo & Sander Granneman & Matthias Thoms & Rizos-Georgios Manikas & David Tollervey & Ed Hurt, 2014. "Coupled GTPase and remodelling ATPase activities form a checkpoint for ribosome export," Nature, Nature, vol. 505(7481), pages 112-116, January.
    • Handle: RePEc:nat:nature:v:505:y:2014:i:7481:d:10.1038_nature12731
    DOI: 10.1038/nature12731
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    Cited by:

    1. Kamil Sekulski & Victor Emmanuel Cruz & Christine S. Weirich & Jan P. Erzberger, 2023. "rRNA methylation by Spb1 regulates the GTPase activity of Nog2 during 60S ribosomal subunit assembly," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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