Outer membrane proteins (OMPs) are essential to gram-negative bacteria, and molecular chaperones prevent the OMPs from aggregation in the periplasm during the OMPs biogenesis. Skp is one of the molecular chaperones for this purpose. Here, we combined single-molecule fluorescence resonance energy transfer and fluorescence correlation spectroscopy to study the affinity and stoichiometric ratio of Skp in its binding with OmpC at the single-molecule level. The half concentration of the Skp self-trimerization (C) was measured to be (2.5 ± 0.7) × 10 nM. Under an Skp concentration far below the C, OmpC could recruit Skp monomers to form OmpC·Skp. The affinity to form the OmpC·Skp complex was determined to be (5.5 ± 0.4) × 10 pM with a Hill coefficient of 1.6 ± 0.2. Under the micromolar concentrations of Skp, the formation of OmpC·(Skp) was confirmed, and the dissociation constant of OmpC·(Skp) was determined to be 1.2 ± 0.4 μM. The precise information will help us to quantitatively depict the role of Skp in the biogenesis of OMPs.
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| http://dx.doi.org/10.1038/s41598-020-71608-4 | DOI Listing |
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