Related Experiment Video
Updated: Mar 11, 2026
09:55
From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
14.2K
Membrane protein insertase YidC in bacteria and archaea
Andreas Kuhn1, Dorothee Kiefer1
1Institute of Microbiology, University of Hohenheim, Stuttgart, 70599, Germany.
Molecular Microbiology
|November 24, 2016
Summary
Prokaryotic membrane protein insertion utilizes Sec translocases and YidC insertases. Recent high-resolution YidC structures reveal mechanisms for protein insertion into the lipid bilayer.
Area of Science:
- Molecular Biology
- Biochemistry
- Structural Biology
Background:
- Protein insertion into prokaryotic plasma membranes is essential for cellular function.
- Translocases (Sec) and insertases (YidC) are key machineries involved in this process.
- Distinct mechanisms are proposed for Sec and YidC in guiding substrate proteins into the lipid bilayer.
Purpose of the Study:
- To elucidate the mechanistic details of YidC-mediated protein insertion.
- To provide new insights into how transmembrane proteins transition from aqueous to hydrophobic environments.
- To leverage high-resolution structural data of YidC for mechanistic understanding.
Main Methods:
- Analysis of recently published high-resolution structures of YidC.
- Comparative analysis of YidC and Sec translocase mechanisms.
- Mechanistic modeling based on structural and biochemical data.
Main Results:
- YidC insertases utilize a groove-like structure at a protein-lipid interface.
- This interaction facilitates the sliding of transmembrane segments into the lipid bilayer.
- Structural insights reveal the transition pathway of proteins from aqueous to hydrophobic membrane environments.
Conclusions:
- High-resolution YidC structures offer significant mechanistic insights into membrane protein insertion.
- YidC employs a distinct mechanism compared to Sec translocases for protein insertion.
- Understanding these mechanisms is crucial for comprehending fundamental cellular processes in prokaryotes.
Related Concept Videos
01:26Insertion of Single-pass Transmembrane Proteins in the RER
18.6K
Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
18.6K
01:45Tail-anchoring of Proteins in the ER Membrane
4.0K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
4.0K
01:26Bacterial Translocation and Protein Secretion
907
Bacterial protein secretion involves translocation systems to ensure proteins reach their designated locations, including the plasma membrane, periplasm, outer membrane, or the external environment. These translocation systems are vital for bacterial physiology, supporting processes like membrane assembly, enzymatic activity in the periplasm, and interactions with the external environment. The division of labor between Sec and Tat pathways ensures efficiency in handling proteins with diverse...
907
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
19.2K
The rough ER membrane synthesizes, assembles, and embeds transmembrane proteins in diverse topologies. These proteins function as transporters or channels and can remain in the ER membrane or are sent to the Golgi complex, lysosome, and cell membrane.
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...
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...
19.2K
01:29Cytoskeletal Proteins in Bacteria
4.4K
Bacterial cells were initially considered simple, randomly organized structures lacking a cytoskeleton. However, the discovery of cytoskeleton homologs in bacteria led to the change of this opinion. Bacterial cytoskeletal filaments regulate the cell shape, cell polarity, cell division, and partitioning of plasmids during cell division. It was later discovered that bacterial cytoskeletal proteins, mainly actin and tubulin homologs, are diverse compared to their eukaryotic counterparts. On the...
4.4K
01:27Plasma Membrane in Bacteria and Archaea
2.6K
The plasma membrane is an essential cellular structure responsible for maintaining cellular integrity and regulating the selective transport of molecules. While bacteria and archaea share the fundamental function of plasma membranes, their structural and molecular differences reflect adaptations to distinct ecological and physiological challenges.Bacterial Plasma MembranesBacterial plasma membranes are predominantly composed of phospholipids with fatty acid chains ester-linked to a glycerol...
2.6K