Related Experiment Video
Updated: May 30, 2026
08:13
Producing Gene Deletions in Escherichia coli by P1 Transduction with Excisable Antibiotic Resistance Cassettes
Published on: September 1, 2018
Role for Escherichia coli YidD in membrane protein insertion
Zhong Yu1, Mariëlle Lavèn, Mirjam Klepsch
1Section of Molecular Microbiology, Department of Molecular Cell Biology, Vrije Universiteit, Amsterdam 1081 HV, Netherlands.
Journal of Bacteriology
|August 2, 2011
Summary
Escherichia coli YidD protein is essential for inner membrane protein insertion and folding. Deleting YidD impaired the function of YidC, a protein involved in membrane protein insertion.
Area of Science:
- Bacterial protein insertion and folding
- Membrane protein biogenesis
- Molecular mechanisms of protein translocation
Background:
- YidC is crucial for bacterial inner membrane protein insertion and folding, but its exact function remains unclear.
- The yidC gene is part of a conserved gene cluster in Gram-negative bacteria, including the upstream yidD gene.
- The yidD gene overlaps with rnpA and is located immediately upstream of yidC.
Purpose of the Study:
- To investigate the role of Escherichia coli YidD in membrane protein insertion and folding.
- To determine the localization and function of YidD in relation to YidC.
- To explore the potential involvement of YidD in the Sec-YidC translocon.
Main Methods:
- Gene expression and protein localization studies of YidD in E. coli.
- Analysis of inner membrane protein insertion and processing in YidD-deficient cells (ΔyidD).
- In vitro cross-linking assays to assess YidD proximity to nascent inner membrane proteins within the Sec-YidC translocon.
Main Results:
- Escherichia coli yidD is expressed and localizes to the inner membrane, likely via an amphipathic helix.
- Inactivation of yidD did not affect cell growth or viability.
- ΔyidD cells exhibited defects in the insertion and processing of three YidC-dependent inner membrane proteins.
- In vitro cross-linking indicated YidD is near nascent inner membrane proteins in the Sec-YidC translocon.
Conclusions:
- YidD plays a significant role in the insertion and processing of specific inner membrane proteins, likely in concert with YidC.
- YidD's localization and proximity to nascent proteins suggest a function within the Sec-YidC translocon machinery.
- Further research is warranted to fully elucidate YidD's precise mechanism in bacterial protein biogenesis.
More Related Videos
Related Concept Videos
01:26Insertion of Single-pass Transmembrane Proteins in the RER
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...
01:28Protein Translocation Machinery on the ER Membrane
The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into 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.
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.
01:29Insertion of Multi-pass Transmembrane Proteins in the RER
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...
01:45Tail-anchoring of Proteins in the ER Membrane
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...
01:26Bacterial Translocation and Protein Secretion
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...
01:34Protein Transport into the Inner Mitochondrial Membrane
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
Transport of mitochondrial precursors across the TIM23 channel is driven by...