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Updated: Aug 11, 2026

Förster Resonance Energy Transfer Mapping: A New Methodology to Elucidate Global Structural Features
Published on: March 16, 2022
Subunit a of cytochrome o oxidase requires both YidC and SecYEG for membrane insertion
David J F du Plessis1, Nico Nouwen, Arnold J M Driessen
1Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Materials Science Center Plus, University of Groningen, 9751 NN Haren, The Netherlands.
Abstract:
The Escherichia coli YidC protein belongs to the Oxa1 family of membrane proteins that facilitate the insertion of membrane proteins. Depletion of YidC in E. coli leads to a specific defect in the functional assembly of major energy transducing complexes such as the F1F0 ATPase and cytochrome bo3 oxidase. Here we report on the in vitro reconstitution of the membrane insertion of the CyoA subunit of cytochrome bo3 oxidase. Efficient insertion of in vitro synthesized pre-CyoA into proteoliposomes requires YidC, SecYEG, and SecA and occurs independently of the proton motive force. These data demonstrate that pre-CyoA is a substrate of a novel pathway that involves both SecYEG and YidC.
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