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Assembly of the Lipid Bilayer in the ER

Assembly of the Lipid Bilayer in the ER

Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

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Published on: July 16, 2020

Assembling of AcrB trimer in cell membrane.

Wei Lu¹, Qian Chai, Meng Zhong

¹Department of Chemistry, University of Kentucky, Lexington, KY 40506, USA.

Journal of Molecular Biology

|July 7, 2012

Summary

Oligomeric membrane proteins like AcrB assemble in Escherichia coli. This study reveals their assembly deviates from random chance, suggesting co-translational clustering influences oligomerization.

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In Vitro Analysis of PDZ-dependent CFTR Macromolecular Signaling Complexes

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Published on: August 13, 2012

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Many essential membrane proteins function as oligomers.
The precise mechanisms of how these protein subunits assemble within the cell membrane are not fully understood.
AcrB, an essential transporter, is known to form an obligate homo-trimer, with folding preceding oligomerization.

Purpose of the Study:

To investigate the assembly mechanism of the AcrB homo-trimer in the Escherichia coli cell membrane.
To determine if AcrB trimerization follows a random subunit association model or if other factors influence the process.
To explore potential explanations for non-random assembly patterns.

Main Methods:

Utilized four experimental approaches involving AcrB variants.
Employed fusion tags, disulfide trapping, and activity measurements to study subunit interactions.
Co-expressed AcrB variants in Escherichia coli to analyze in vivo assembly.

Main Results:

Demonstrated that co-expressed AcrB variants can form hybrid trimers within the same cell.
Observed that the extent of co-assembly did not align with predictions based on a random subunit association model.
Identified a deviation from random assembling, suggesting non-random factors are at play.

Conclusions:

AcrB homo-trimerization in vivo is not solely driven by random subunit encounters.
The polysome structure during translation may play a role in clustering subunits, influencing their assembly.
These findings offer novel insights into the dynamic assembly and equilibration of obligate homo-oligomeric membrane proteins.