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The SecA motor generates mechanical force during protein translocation

Author

Listed:
  • Riti Gupta

    (Johns Hopkins University)

  • Dmitri Toptygin

    (Johns Hopkins University)

  • Christian M. Kaiser

    (Johns Hopkins University
    Johns Hopkins University)

Abstract

The Sec translocon moves proteins across lipid bilayers in all cells. The Sec channel enables passage of unfolded proteins through the bacterial plasma membrane, driven by the cytosolic ATPase SecA. Whether SecA generates mechanical force to overcome barriers to translocation posed by structured substrate proteins is unknown. Here, we kinetically dissect Sec-dependent translocation by monitoring translocation of a folded substrate protein with tunable stability at high time resolution. We find that substrate unfolding constitutes the rate-limiting step during translocation. Using single-molecule force spectroscopy, we also define the response of the protein to mechanical force. Relating the kinetic and force measurements reveals that SecA generates at least 10 piconewtons of mechanical force to actively unfold translocating proteins, comparable to cellular unfoldases. Combining biochemical and single-molecule measurements thus allows us to define how the SecA motor ensures efficient and robust export of proteins that contain stable structure.

Suggested Citation

  • Riti Gupta & Dmitri Toptygin & Christian M. Kaiser, 2020. "The SecA motor generates mechanical force during protein translocation," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17561-2
    DOI: 10.1038/s41467-020-17561-2
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    Cited by:

    1. Zikun Zhu & Shuai Wang & Shu-ou Shan, 2022. "Ribosome profiling reveals multiple roles of SecA in cotranslational protein export," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Han Wang & Guojun Chen & Hongbin Li, 2022. "Templated folding of the RTX domain of the bacterial toxin adenylate cyclase revealed by single molecule force spectroscopy," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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