AI Article Synopsis
- Outer membrane proteins (OMPs) play critical roles in Gram-negative bacteria by serving as receptors, transporters, and channels for various substances.
- The folding and assembly of OMPs require the collaboration of chaperones and protein complexes to ensure these proteins reach the outer membrane correctly.
- Current research emphasizes the need to understand how these molecular machines function based on thermodynamics instead of the usual ATP energy source, and single-molecule studies may provide valuable insights into this process.
Article Abstract
Outer membrane proteins (OMPs) maintain the viability of Gram-negative bacteria by functioning as receptors, transporters, ion channels, lipases, and porins. Folding and assembly of OMPs involves synchronized action of chaperones and multi-protein machineries which escort the highly hydrophobic polypeptides to their target outer membrane in a folding competent state. Previous studies have identified proteins and their involvement along the OMP biogenesis pathway. Yet, the mechanisms of action and the intriguing ability of all these molecular machines to work without the typical cellular energy source of ATP, but solely based on thermodynamic principles, are still not well understood. Here, we highlight how different single-molecule studies can shed additional light on the mechanisms and kinetics of OMP biogenesis.
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| http://dx.doi.org/10.1002/bies.202200149 | DOI Listing |
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