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The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn

Author

Listed:
  • F. Esra Demircioglu

    (Massachusetts Institute of Technology)

  • Weili Zheng

    (University of Virginia)

  • Alexander J. McQuown

    (Harvard University)

  • Nolan K. Maier

    (Massachusetts Institute of Technology
    Whitehead Institute for Biomedical Research)

  • Nicki Watson

    (The Whitehead Institute)

  • Iain M. Cheeseman

    (Massachusetts Institute of Technology
    Whitehead Institute for Biomedical Research)

  • Vladimir Denic

    (Harvard University)

  • Edward H. Egelman

    (University of Virginia)

  • Thomas U. Schwartz

    (Massachusetts Institute of Technology)

Abstract

TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator. Also, it likely does not thread a peptide substrate through a narrow central channel, in contrast to its closest structural homologs. Here, we examined the oligomerization of TorsinA to get closer to a molecular understanding of its still enigmatic function. We observe TorsinA to form helical filaments, which we analyzed by cryo-electron microscopy using helical reconstruction. The 4.4 Å structure reveals long hollow tubes with a helical periodicity of 8.5 subunits per turn, and an inner channel of ~ 4 nm diameter. We further show that the protein is able to induce tubulation of membranes in vitro, an observation that may reflect an entirely new characteristic of AAA + ATPases. We discuss the implications of these observations for TorsinA function.

Suggested Citation

  • F. Esra Demircioglu & Weili Zheng & Alexander J. McQuown & Nolan K. Maier & Nicki Watson & Iain M. Cheeseman & Vladimir Denic & Edward H. Egelman & Thomas U. Schwartz, 2019. "The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11194-w
    DOI: 10.1038/s41467-019-11194-w
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