Related Experiment Video
Updated: Jul 3, 2026

Co-Translational Insertion of Membrane Proteins into Preformed Nanodiscs
Published on: November 19, 2020
Mechanisms of YidC-mediated insertion and assembly of multimeric membrane protein complexes
Stefan Kol1, Nico Nouwen, Arnold J M Driessen
1Department of Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, the Zernike Institute of Advanced Materials, The Netherlands.
Abstract:
The YidC protein fulfills a dual and essential role in the assembly of inner membrane proteins in Escherichia coli. Besides interacting with transmembrane segments of newly synthesized membrane proteins that insert into the membrane via the SecYEG complex, YidC also functions as an independent membrane protein insertase and assists in membrane protein folding. Here, we discuss the mechanisms of YidC substrate recognition and membrane insertion with emphasis on its role in the assembly of multimeric membrane protein complexes such as the F1F0-ATP synthase.
Related Concept Videos
Mechanisms of Membrane Domain Formation
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Protein Translocation Machinery on the ER Membrane
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...

