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Related Experiment Video

Updated: Feb 10, 2026

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
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Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs

Published on: November 19, 2020

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YidC-mediated membrane insertion.

Dorothee Kiefer1, Andreas Kuhn1

  • 1Department of Microbiology, University of Hohenheim, Garbenstrasse 30, 70599 Stuttgart, Germany.

FEMS Microbiology Letters
|May 26, 2018
PubMed
Summary

The YidC insertase, a single protein, efficiently integrates membrane proteins into lipid bilayers. It also aids in protein folding, operating independently or with other systems like SecYEG.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Membrane Biology

Background:

  • The YidC/Oxa/Alb insertase is a universal, single-protein catalyst for membrane protein insertion found across archaea, bacteria, and eukaryotic organelles.
  • In bacteria, YidC facilitates the insertion of small membrane proteins independently and larger ones with the SecYEG translocase.
  • Mitochondrial Oxa, a YidC homolog, inserts all matrix-synthesized membrane proteins due to the absence of Sec homologues.

Purpose of the Study:

  • To investigate the mechanism of YidC-mediated membrane protein insertion and folding.
  • To explore YidC's independent function in membrane protein integration.

Main Methods:

  • Reconstitution of YidC into liposomes for in vitro studies.
  • Single molecule force spectroscopy to analyze protein-lipid interactions and folding dynamics.

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Main Results:

  • YidC rapidly and efficiently binds substrate proteins and integrates them into the lipid bilayer.
  • YidC binds unfolded membrane proteins and promotes their folding into the membrane.
  • Evidence suggests YidC can function independently of the SecYEG translocase.

Conclusions:

  • YidC is a versatile and efficient catalyst for membrane protein insertion and folding.
  • The mechanism involves YidC facilitating the translocation of substrate periplasmic regions across the membrane.
  • Further research is needed to fully elucidate the YidC-mediated insertion pathway.