
pmid: 12522254
After transport across the cytoplasmic membrane, bacterial outer membrane proteins are assembled into the outer membrane. Meningococcal Omp85 is a highly conserved protein in Gram-negative bacteria, and its homolog Toc75 is a component of the chloroplast protein-import machinery. Omp85 appeared to be essential for viability, and unassembled forms of various outer membrane proteins accumulated upon Omp85 depletion. Immunofluorescence microscopy revealed decreased surface exposure of outer membrane proteins, which was particularly apparent at the cell-division planes. Thus, Omp85 is likely to play a role in outer membrane protein assembly.
Isopropyl Thiogalactoside, Lipopolysaccharides, Cell biology, Protein Denaturation, Protein Folding, Molecular biology, Cell Membrane, Molecular Sequence Data, Porins, Neisseria meningitidis, Life sciences, Microbiology, Phospholipases A, Phospholipases A1, Protein Structure, Tertiary, Protein Transport, Biologie/Milieukunde (BIOL), Microscopy, Fluorescence, Amino Acid Sequence, Fimbriae Proteins, Conserved Sequence, Bacterial Outer Membrane Proteins
Isopropyl Thiogalactoside, Lipopolysaccharides, Cell biology, Protein Denaturation, Protein Folding, Molecular biology, Cell Membrane, Molecular Sequence Data, Porins, Neisseria meningitidis, Life sciences, Microbiology, Phospholipases A, Phospholipases A1, Protein Structure, Tertiary, Protein Transport, Biologie/Milieukunde (BIOL), Microscopy, Fluorescence, Amino Acid Sequence, Fimbriae Proteins, Conserved Sequence, Bacterial Outer Membrane Proteins
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