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Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines

Author

Listed:
  • Andreas Martin

    (Howard Hughes Medical Institute, Massachusetts Institute of Technology)

  • Tania A. Baker

    (Howard Hughes Medical Institute, Massachusetts Institute of Technology
    Howard Hughes Medical Institute, Massachusetts Institute of Technology)

  • Robert T. Sauer

    (Howard Hughes Medical Institute, Massachusetts Institute of Technology)

Abstract

Hexameric ring-shaped ATPases of the AAA + (for ATPases associated with various cellular activities) superfamily power cellular processes in which macromolecular structures and complexes are dismantled or denatured, but the mechanisms used by these machine-like enzymes are poorly understood. By covalently linking active and inactive subunits of the ATPase ClpX to form hexamers, here we show that diverse geometric arrangements can support the enzymatic unfolding of protein substrates and translocation of the denatured polypeptide into the ClpP peptidase for degradation. These studies indicate that the ClpX power stroke is generated by ATP hydrolysis in a single subunit, rule out concerted and strict sequential ATP hydrolysis models, and provide evidence for a probabilistic sequence of nucleotide hydrolysis. This mechanism would allow any ClpX subunit in contact with a translocating polypeptide to hydrolyse ATP to drive substrate spooling into ClpP, and would prevent stalling if one subunit failed to bind or hydrolyse ATP. Energy-dependent machines with highly diverse quaternary architectures and molecular functions could operate by similar asymmetric mechanisms.

Suggested Citation

  • Andreas Martin & Tania A. Baker & Robert T. Sauer, 2005. "Rebuilt AAA + motors reveal operating principles for ATP-fuelled machines," Nature, Nature, vol. 437(7062), pages 1115-1120, October.
  • Handle: RePEc:nat:nature:v:437:y:2005:i:7062:d:10.1038_nature04031
    DOI: 10.1038/nature04031
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    Cited by:

    1. Doan Tuong-Van Le & Thomas Eckert & Günther Woehlke, 2013. "Computer Simulation of Assembly and Co-operativity of Hexameric AAA ATPases," PLOS ONE, Public Library of Science, vol. 8(7), pages 1-19, July.
    2. Andrea N Kravats & Sam Tonddast-Navaei & George Stan, 2016. "Coarse-Grained Simulations of Topology-Dependent Mechanisms of Protein Unfolding and Translocation Mediated by ClpY ATPase Nanomachines," PLOS Computational Biology, Public Library of Science, vol. 12(1), pages 1-24, January.
    3. Alireza Ghanbarpour & Steven E. Cohen & Xue Fei & Laurel F. Kinman & Tristan A. Bell & Jia Jia Zhang & Tania A. Baker & Joseph H. Davis & Robert T. Sauer, 2023. "A closed translocation channel in the substrate-free AAA+ ClpXP protease diminishes rogue degradation," Nature Communications, Nature, vol. 14(1), pages 1-10, December.
    4. Anthony D. Rish & Zhangfei Shen & Zhenhang Chen & Nan Zhang & Qingfei Zheng & Tian-Min Fu, 2023. "Molecular mechanisms of Holliday junction branch migration catalyzed by an asymmetric RuvB hexamer," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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