Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacterial Outer Membrane Proteins / chemistry
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Bacterial Outer Membrane Proteins / genetics
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Bacterial Outer Membrane Proteins / metabolism*
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Bacterial Outer Membrane Proteins / physiology*
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Cell Membrane / metabolism*
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Conserved Sequence
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Fimbriae Proteins / metabolism
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Isopropyl Thiogalactoside / pharmacology
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Lipopolysaccharides / metabolism
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Microscopy, Fluorescence
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Molecular Sequence Data
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Neisseria meningitidis / genetics
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Neisseria meningitidis / growth & development
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Neisseria meningitidis / metabolism*
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Phospholipases A / chemistry
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Phospholipases A / metabolism
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Phospholipases A1
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Porins / metabolism
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Protein Denaturation
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Protein Folding
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Protein Structure, Tertiary
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Protein Transport
Substances
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Bacterial Outer Membrane Proteins
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Lipopolysaccharides
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Omp85 protein, Neisseria
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Porins
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pilQ protein, bacteria
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porin protein, Neisseria
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Fimbriae Proteins
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Isopropyl Thiogalactoside
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Phospholipases A
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Phospholipases A1
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outer membrane phospholipase A