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Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly
TLDR
Immunofluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes, and Omp85 is likely to play a role in outer membrane protein assembly. Expand
Structure of the translocator domain of a bacterial autotransporter
TLDR
The crystal structure of the in vitro‐folded translocator domain of the autotransporter NalP from Neisseria meningitidis is presented, which reveals a 12‐stranded β‐barrel with a hydrophilic pore of 10 × 12.5 Å that is filled by an N‐terminal α‐helix that has pore activity in vivo and in vitro. Expand
Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif
TLDR
Results demonstrate that the Omp85 assembly machinery recognizes OMPs by virtue of their C-terminal signature sequence. Expand
Biogenesis of the gram-negative bacterial outer membrane.
TLDR
The cell envelope of gram-negative bacteria consists of two membranes, the inner and the outer membrane, that are separated by the periplasm, that have to be transported across the inner membrane and through theperiplasm to assemble eventually in the correct membrane. Expand
Involvement of stress protein PspA (phage shock protein A) of Escherichia coli in maintenance of the protonmotive force under stress conditions.
TLDR
Quantitative in vivo determination of the deltamu H+ showed that it specifically decreased in a pspA mutant strain upon expression of plasmid‐encoded (mutant) prePhoE protein, indicating that only PspA is required for efficient translocation. Expand
Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
TLDR
The outer membrane protein, XcpQ, which is involved in transport of folded proteins across the outer membrane of P. aeruginosa, was purified as a highly stable homomultimer and revealed large, ring‐shaped structures with an apparent central cavity of 95 Å. Expand
Interactions between Phage-Shock Proteins in Escherichia coli
TLDR
Data indicate that regulation of the psp operon is mediated via protein-protein interactions, and that PspD localizes as a peripherally bound inner membrane protein. Expand
Role of the Pilot Protein YscW in the Biogenesis of the YscC Secretin in Yersinia enterocolitica
TLDR
YscW interacts with the unassembled YscC protein and facilitates efficient oligomerization, likely at the outer membrane, confirming the function of YscW as a pilot protein. Expand
The C Terminus of SecA Is Involved in Both Lipid Binding and SecB Binding (*)
TLDR
The observation that the SecA mutant protein lacking the C-terminal 70 residues had a strongly reduced ability to mediate binding of SecB-precursor complexes to inverted inner membrane vesicles demonstrates that the C terminus of SecA is also involved in SecB binding. Expand
Functioning of outer membrane protein assembly factor Omp85 requires a single POTRA domain
TLDR
The functional core of bacterial Omp85 consists of its membrane domain and a single POTra domain, that is, POTRA5, similar to the mitochondrial Omp 85 homologue. Expand
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