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A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
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Translocation of proteins across membranes is an ancient process that occurs even in bacteria and archaebacteria. In fact, the components of the translocation machinery are still conserved between prokaryotes and eukaryotes.
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Lipids Activate SecA for High Affinity Binding to the SecYEG Complex.

Sabrina Koch1, Janny G de Wit1, Iuliia Vos1

  • 1From the Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and Zernike Institute for Advanced Materials and.

The Journal of Biological Chemistry
|September 11, 2016
PubMed
Summary
This summary is machine-generated.

SecA protein translocation relies on lipid binding to the SecYEG complex. Acidic phospholipids activate SecA, enabling ATP-dependent protein transport across bacterial membranes.

Keywords:
SecASecYEGapolipoproteinlipid bilayermembrane biophysicsmembrane functionmembrane proteinnanodiscsprotein-lipid interactionscaffold protein

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein translocation across the bacterial cytoplasmic membrane is vital.
  • The Sec translocase, including SecYEG, SecA, and SecDFyajC, mediates this process.
  • Anionic lipids are known to be essential for SecA activity.

Purpose of the Study:

  • To elucidate the role of lipid binding in SecA's interaction with the SecYEG complex.
  • To understand how lipids influence SecA activity during protein translocation.

Main Methods:

  • Utilized nanodiscs reconstituted with single SecYEG complexes.
  • Varied lipid composition within the nanodiscs.
  • Investigated SecA's interaction and activation mechanisms.

Main Results:

  • SecA accesses the SecYEG complex through a lipid-bound intermediate state.
  • Acidic phospholipids allosterically activate SecA.
  • This activation is crucial for ATP-dependent protein translocation.

Conclusions:

  • Lipid binding is a prerequisite for SecA's interaction with SecYEG.
  • Specific lipid interactions, particularly with acidic phospholipids, regulate SecA function.
  • This provides mechanistic insight into bacterial protein transport.