The Trimeric Periplasmic Chaperone Skp of Escherichia coli Forms 1:1 Complexes with Outer Membrane Proteins via Hydrophobic and Electrostatic Interactions

The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions.

The interactions of outer membrane proteins (OMPs) with the periplasmic chaperone Skp from Escherichia coli are not well understood. We have examined the binding of Skp to various OMPs of different origin, size, and function. These were OmpA, OmpG, and YaeT (Omp85) from Escherichia coli, the translocator domain of the autotransporter NalP from Neisseria meningitides, FomA from Fusobacterium nuc...

The Trimeric Periplasmic Chaperone Skp of Escherichia coli Forms 1:1 Complexes with Outer Membrane Proteins via Hydrophobic and Electostatic Interactions

*Corresponding author. E-mail addr Abbreviations used: BSA, bovine hVDAC1, voltage-dependent aniondomain of the autotransporter NalP OmpA, outer membrane protein A o isomerases; SurA, the survival factor WT-OmpA, wild type OmpA; YaeT The interactions of outer membrane proteins (OMPs) with the periplasmic chaperone Skp from Escherichia coli are not well understood. We have examined the binding o...

The interactions of outer membrane proteins with the periplasmic chaperone Skp of E.coli and with LPS

Direct Observation of the Uptake of Outer Membrane Proteins by the Periplasmic Chaperone Skp

The transportation of membrane proteins through the aqueous subcellular space is an important and challenging process. Its molecular mechanism and the associated structural change are poorly understood. Periplasmic chaperones, such as Skp in Escherichia coli, play key roles in the transportation and protection of outer membrane proteins (OMPs) in Gram-negative bacteria. The molecular mechanism ...

The early interaction of the outer membrane protein phoe with the periplasmic chaperone Skp occurs at the cytoplasmic membrane.

Spheroplasts were used to study the early interactions of newly synthesized outer membrane protein PhoE with periplasmic proteins employing a protein cross-linking approach. Newly translocated PhoE protein could be cross-linked to the periplasmic chaperone Skp at the periplasmic side of the inner membrane. To study the timing of this interaction, a PhoE-dihydrofolate reductase hybrid protein wa...