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Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7

Author

Listed:
  • Yu-Hua Lo

    (111T. W. Alexander Drive)

  • Mack Sobhany

    (111T. W. Alexander Drive)

  • Allen L. Hsu

    (111T. W. Alexander Drive)

  • Brittany L. Ford

    (111T. W. Alexander Drive)

  • Juno M. Krahn

    (111T. W. Alexander Drive)

  • Mario J. Borgnia

    (111T. W. Alexander Drive)

  • Robin E. Stanley

    (111T. W. Alexander Drive)

Abstract

Rix7 is an essential type II AAA-ATPase required for the formation of the large ribosomal subunit. Rix7 has been proposed to utilize the power of ATP hydrolysis to drive the removal of assembly factors from pre-60S particles, but the mechanism of release is unknown. Rix7’s mammalian homolog, NVL2 has been linked to cancer and mental illness disorders, highlighting the need to understand the molecular mechanisms of this essential machine. Here we report the cryo-EM reconstruction of the tandem AAA domains of Rix7 which form an asymmetric stacked homohexameric ring. We trapped Rix7 with a polypeptide in the central channel, revealing Rix7’s role as a molecular unfoldase. The structure establishes that type II AAA-ATPases lacking the aromatic-hydrophobic motif within the first AAA domain can engage a substrate throughout the entire central channel. The structure also reveals that Rix7 contains unique post-α7 insertions within both AAA domains important for Rix7 function.

Suggested Citation

  • Yu-Hua Lo & Mack Sobhany & Allen L. Hsu & Brittany L. Ford & Juno M. Krahn & Mario J. Borgnia & Robin E. Stanley, 2019. "Cryo-EM structure of the essential ribosome assembly AAA-ATPase Rix7," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08373-0
    DOI: 10.1038/s41467-019-08373-0
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    Cited by:

    1. Ian Cooney & Heidi L. Schubert & Karina Cedeno & Olivia N. Fisher & Richard Carson & John C. Price & Christopher P. Hill & Peter S. Shen, 2024. "Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    2. Jingyu Zhan & Allison Zeher & Rick Huang & Wai Kwan Tang & Lisa M. Jenkins & Di Xia, 2024. "Conformations of Bcs1L undergoing ATP hydrolysis suggest a concerted translocation mechanism for folded iron-sulfur protein substrate," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    3. Yang Xu & Han Han & Ian Cooney & Yuxuan Guo & Noah G. Moran & Nathan R. Zuniga & John C. Price & Christopher P. Hill & Peter S. Shen, 2022. "Active conformation of the p97-p47 unfoldase complex," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
    4. Maximilian Rüttermann & Michelle Koci & Pascal Lill & Ermis Dionysios Geladas & Farnusch Kaschani & Björn Udo Klink & Ralf Erdmann & Christos Gatsogiannis, 2023. "Structure of the peroxisomal Pex1/Pex6 ATPase complex bound to a substrate," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    5. Jakob M. Silberberg & Sophie Ketter & Paul J. N. Böhm & Kristin Jordan & Marcel Wittenberg & Julia Grass & Inga Hänelt, 2024. "KdpD is a tandem serine histidine kinase that controls K+ pump KdpFABC transcriptionally and post-translationally," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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