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Lipids activate SecA for high affinity binding to the SecYEG complex

Journal Article


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Abstract


  • Protein translocation across the bacterial cytoplasmic membraneis an essential process catalyzed predominantly bythe Sec translocase. This system consists of the membrane-embedded protein-conducting channel SecYEG, the motor ATPase SecA, and the heterotrimeric SecDFyajC membrane protein complex. Previous studies suggest that anionic lipids are essential for SecA activity and that the N terminus of SecA is capable of penetrating the lipid bilayer. The role of lipid binding, however, has remained elusive. By employing differently sized nanodiscs reconstituted with single SecYEG complexes and comprising varying amounts of lipids, we establish that SecA gains access to the SecYEG complex via a lipid-bound intermediate state, whereas acidic phospholipids allosterically activate SecA for ATP-dependent protein translocation.

Authors


  •   Koch, Sabrina (external author)
  •   De Wit, Janny (external author)
  •   Vos, Iuliia (external author)
  •   Birkner, Jan (external author)
  •   Gordiichuk, Pavlo (external author)
  •   Herrmann, Andreas (external author)
  •   van Oijen, Antoine M.
  •   Driessen, Arnold J. (external author)

Publication Date


  • 2016

Citation


  • Koch, S., De Wit, J., Vos, I., Birkner, J., Gordiichuk, P., Herrmann, A., van Oijen, A. M. & Driessen, A. J. (2016). Lipids activate SecA for high affinity binding to the SecYEG complex. Journal of Biological Chemistry, 291 (43), 22534-22543.

Scopus Eid


  • 2-s2.0-84992431213

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5230&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/4206

Number Of Pages


  • 9

Start Page


  • 22534

End Page


  • 22543

Volume


  • 291

Issue


  • 43

Abstract


  • Protein translocation across the bacterial cytoplasmic membraneis an essential process catalyzed predominantly bythe Sec translocase. This system consists of the membrane-embedded protein-conducting channel SecYEG, the motor ATPase SecA, and the heterotrimeric SecDFyajC membrane protein complex. Previous studies suggest that anionic lipids are essential for SecA activity and that the N terminus of SecA is capable of penetrating the lipid bilayer. The role of lipid binding, however, has remained elusive. By employing differently sized nanodiscs reconstituted with single SecYEG complexes and comprising varying amounts of lipids, we establish that SecA gains access to the SecYEG complex via a lipid-bound intermediate state, whereas acidic phospholipids allosterically activate SecA for ATP-dependent protein translocation.

Authors


  •   Koch, Sabrina (external author)
  •   De Wit, Janny (external author)
  •   Vos, Iuliia (external author)
  •   Birkner, Jan (external author)
  •   Gordiichuk, Pavlo (external author)
  •   Herrmann, Andreas (external author)
  •   van Oijen, Antoine M.
  •   Driessen, Arnold J. (external author)

Publication Date


  • 2016

Citation


  • Koch, S., De Wit, J., Vos, I., Birkner, J., Gordiichuk, P., Herrmann, A., van Oijen, A. M. & Driessen, A. J. (2016). Lipids activate SecA for high affinity binding to the SecYEG complex. Journal of Biological Chemistry, 291 (43), 22534-22543.

Scopus Eid


  • 2-s2.0-84992431213

Ro Full-text Url


  • http://ro.uow.edu.au/cgi/viewcontent.cgi?article=5230&context=smhpapers

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers/4206

Number Of Pages


  • 9

Start Page


  • 22534

End Page


  • 22543

Volume


  • 291

Issue


  • 43